메뉴 건너뛰기




Volumn 8, Issue 3, 2015, Pages 366-415

Peptides and peptidomimetics for antimicrobial drug design

Author keywords

Antimicrobial peptides; Mechanism of action; Peptidomimetics

Indexed keywords

ALPHA DEFENSIN; BETA DEFENSIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CECROPIN; INDOLICIDIN; LYSOSTAPHIN; MELITTIN; MUTACIN 1140; NISIN; POLYPEPTIDE ANTIBIOTIC AGENT; THIONIN PEPTIDE; UNCLASSIFIED DRUG;

EID: 84937921183     PISSN: None     EISSN: 14248247     Source Type: Journal    
DOI: 10.3390/ph8030366     Document Type: Review
Times cited : (179)

References (311)
  • 2
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • Wimley, W.C. Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem. Biol. 2010, 5, 905-917.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 3
    • 84878419915 scopus 로고    scopus 로고
    • Database-guided discovery of potent peptides to combat hiv-1 or superbugs
    • Wang, G. Database-guided discovery of potent peptides to combat hiv-1 or superbugs. Pharmaceuticals (Basel) 2013, 6, 728-758.
    • (2013) Pharmaceuticals (Basel) , vol.6 , pp. 728-758
    • Wang, G.1
  • 4
    • 57749088664 scopus 로고    scopus 로고
    • Structures of human host defense cathelicidin ll-37 and its smallest antimicrobial peptide kr-12 in lipid micelles
    • Wang, G. Structures of human host defense cathelicidin ll-37 and its smallest antimicrobial peptide kr-12 in lipid micelles. J. Biol. Chem. 2008, 283, 32637-32643.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32637-32643
    • Wang, G.1
  • 5
    • 2342593248 scopus 로고    scopus 로고
    • Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin i
    • Powers, J.P.; Rozek, A.; Hancock, R.E. Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin i. Biochim. Biophys. Acta 2004, 1698, 239-250.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 239-250
    • Powers, J.P.1    Rozek, A.2    Hancock, R.E.3
  • 6
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • Rozek, A.; Friedrich, C.L.; Hancock, R.E. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 2000, 39, 15765-15774.
    • (2000) Biochemistry , vol.39 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.3
  • 8
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • Andreu, D.; Rivas, L. Animal antimicrobial peptides: An overview. Biopolymers 1998, 47, 415-433.
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 9
    • 58149187882 scopus 로고    scopus 로고
    • Apd2: The updated antimicrobial peptide database and its application in peptide design
    • Wang, G.; Li, X.; Wang, Z. Apd2: The updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009, 37, D933-D937.
    • (2009) Nucleic Acids Res. , vol.37 , pp. D933-D937
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 10
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner, H.; Hultmark, D.; Engstrom, A.; Bennich, H.; Boman, H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 1981, 292, 246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 11
    • 84860601877 scopus 로고    scopus 로고
    • Antimicrobial peptides: Key components of the innate immune system
    • Pasupuleti, M.; Schmidtchen, A.; Malmsten, M. Antimicrobial peptides: Key components of the innate immune system. Crit. Rev. Biotechnol. 2012, 32, 143-171.
    • (2012) Crit. Rev. Biotechnol. , vol.32 , pp. 143-171
    • Pasupuleti, M.1    Schmidtchen, A.2    Malmsten, M.3
  • 12
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, H.G. Peptide antibiotics and their role in innate immunity. Ann. Rev. immunol. 1995, 13, 61-92.
    • (1995) Ann. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 14
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted, M.E.; Ouellette, A.J. Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 2005, 6, 551-557.
    • (2005) Nat. Immunol. , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 15
    • 0025066842 scopus 로고
    • Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins
    • Skerlavaj, B.; Romeo, D.; Gennaro, R. Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins. Infect. Immun. 1990, 58, 3724-3730.
    • (1990) Infect. Immun. , vol.58 , pp. 3724-3730
    • Skerlavaj, B.1    Romeo, D.2    Gennaro, R.3
  • 18
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz, T. Defensins: Antimicrobial peptides of innate immunity. Nature Rev. Immunol. 2003, 3, 710-720.
    • (2003) Nature Rev. Immunol. , vol.3 , pp. 710-720
    • Ganz, T.1
  • 21
    • 0029819784 scopus 로고    scopus 로고
    • Paneth cell defensins: Endogenous peptide components of intestinal host defense
    • Ouellette, A.J.; Selsted, M.E. Paneth cell defensins: Endogenous peptide components of intestinal host defense. FASEB J. 1996, 10, 1280-1289.
    • (1996) FASEB J. , vol.10 , pp. 1280-1289
    • Ouellette, A.J.1    Selsted, M.E.2
  • 23
    • 11244342346 scopus 로고    scopus 로고
    • Antibacterial activity and specificity of the six human {alpha}-defensins
    • Ericksen, B.; Wu, Z.; Lu, W.; Lehrer, R.I. Antibacterial activity and specificity of the six human {alpha}-defensins. Antimicrob. Agents Chemother. 2005, 49, 269-275.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 269-275
    • Ericksen, B.1    Wu, Z.2    Lu, W.3    Lehrer, R.I.4
  • 24
    • 0030913746 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity of human intestinal defensin 5
    • Porter, E.M.; van Dam, E.; Valore, E.V.; Ganz, T. Broad-spectrum antimicrobial activity of human intestinal defensin 5. Infect. Immun. 1997, 65, 2396-2401.
    • (1997) Infect. Immun. , vol.65 , pp. 2396-2401
    • Porter, E.M.1    van Dam, E.2    Valore, E.V.3    Ganz, T.4
  • 25
    • 33747735624 scopus 로고    scopus 로고
    • High-level production of bioactive human beta-defensin-4 in escherichia coli by soluble fusion expression
    • Xu, Z.; Zhong, Z.; Huang, L.; Peng, L.; Wang, F.; Cen, P. High-level production of bioactive human beta-defensin-4 in escherichia coli by soluble fusion expression. Appl. Microbiol. Biotechnol. 2006, 72, 471-479.
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 471-479
    • Xu, Z.1    Zhong, Z.2    Huang, L.3    Peng, L.4    Wang, F.5    Cen, P.6
  • 27
    • 0036135697 scopus 로고    scopus 로고
    • Cathelicidins: A family of endogenous antimicrobial peptides
    • Lehrer, R.I.; Ganz, T. Cathelicidins: A family of endogenous antimicrobial peptides. Curr. Opin. Hematol. 2002, 9, 18-22.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 18-22
    • Lehrer, R.I.1    Ganz, T.2
  • 28
    • 0036379140 scopus 로고    scopus 로고
    • Cathelicidins, essential gene-encoded mammalian antibiotics
    • Zaiou, M.; Gallo, R.L. Cathelicidins, essential gene-encoded mammalian antibiotics. J. Mol. Med. (Berl) 2002, 80, 549-561.
    • (2002) J. Mol. Med. (Berl) , vol.80 , pp. 549-561
    • Zaiou, M.1    Gallo, R.L.2
  • 30
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus kostmann: An observation study
    • Putsep, K.; Carlsson, G.; Boman, H.G.; Andersson, M. Deficiency of antibacterial peptides in patients with morbus kostmann: An observation study. Lancet 2002, 360, 1144-1149.
    • (2002) Lancet , vol.360 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.G.3    Andersson, M.4
  • 31
    • 33751545243 scopus 로고    scopus 로고
    • Crystal structures of human alpha-defensins hnp4, hd5, and hd6
    • Szyk, A.; Wu, Z.; Tucker, K.; Yang, D.; Lu, W.; Lubkowski, J. Crystal structures of human alpha-defensins hnp4, hd5, and hd6. Protein Sci. 2006, 15, 2749-2760.
    • (2006) Protein Sci. , vol.15 , pp. 2749-2760
    • Szyk, A.1    Wu, Z.2    Tucker, K.3    Yang, D.4    Lu, W.5    Lubkowski, J.6
  • 32
    • 0035914442 scopus 로고    scopus 로고
    • The structure of human beta-defensin-1: New insights into structural properties of beta-defensins
    • Hoover, D.M.; Chertov, O.; Lubkowski, J. The structure of human beta-defensin-1: New insights into structural properties of beta-defensins. J. Biol. Chem. 2001, 276, 39021-39026.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39021-39026
    • Hoover, D.M.1    Chertov, O.2    Lubkowski, J.3
  • 33
    • 0035836463 scopus 로고    scopus 로고
    • Three-dimensional structure of rtd-1, a cyclic antimicrobial defensin from rhesus macaque leukocytes
    • Trabi, M.; Schirra, H.J.; Craik, D.J. Three-dimensional structure of rtd-1, a cyclic antimicrobial defensin from rhesus macaque leukocytes. Biochemistry 2001, 40, 4211-4221.
    • (2001) Biochemistry , vol.40 , pp. 4211-4221
    • Trabi, M.1    Schirra, H.J.2    Craik, D.J.3
  • 34
    • 9444225012 scopus 로고    scopus 로고
    • Mode of action of the antimicrobial peptide indolicidin
    • Falla, T.J.; Karunaratne, D.N.; Hancock, R.E.W. Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 1996, 271, 19298-19303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19298-19303
    • Falla, T.J.1    Karunaratne, D.N.2    Hancock, R.E.W.3
  • 36
    • 23044452974 scopus 로고    scopus 로고
    • Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: Evidence for multiple conformations involved in binding to membranes and DNA
    • Hsu, C.H.; Chen, C.; Jou, M.L.; Lee, A.Y.; Lin, Y.C.; Yu, Y.P.; Huang, W.T.; Wu, S.H. Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: Evidence for multiple conformations involved in binding to membranes and DNA. Nucleic Acids Res. 2005, 33, 4053-4064.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4053-4064
    • Hsu, C.H.1    Chen, C.2    Jou, M.L.3    Lee, A.Y.4    Lin, Y.C.5    Yu, Y.P.6    Huang, W.T.7    Wu, S.H.8
  • 37
    • 0032031434 scopus 로고    scopus 로고
    • Mechanism of antimicrobial action of indolicidin
    • Subbalakshmi, C.; Sitaram, N. Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett. 1998, 160, 91-96.
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 91-96
    • Subbalakshmi, C.1    Sitaram, N.2
  • 38
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of escherichia coli
    • Wu, M.; Maier, E.; Benz, R.; Hancock, R.E. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of escherichia coli. Biochemistry 1999, 38, 7235-7242.
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.4
  • 40
    • 7444240737 scopus 로고    scopus 로고
    • New indolicidin analogues with potent antibacterial activity
    • Ryge, T.S.; Doisy, X.; Ifrah, D.; Olsen, J.E.; Hansen, P.R. New indolicidin analogues with potent antibacterial activity. J. Pept. Res. 2004, 64, 171-185.
    • (2004) J. Pept. Res. , vol.64 , pp. 171-185
    • Ryge, T.S.1    Doisy, X.2    Ifrah, D.3    Olsen, J.E.4    Hansen, P.R.5
  • 41
    • 0035968224 scopus 로고    scopus 로고
    • Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria
    • Friedrich, C.L.; Rozek, A.; Patrzykat, A.; Hancock, R.E. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria. J. Biol. Chem. 2001, 276, 24015-24022.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24015-24022
    • Friedrich, C.L.1    Rozek, A.2    Patrzykat, A.3    Hancock, R.E.4
  • 42
    • 0030997215 scopus 로고    scopus 로고
    • Improved activity of a synthetic indolicidin analog
    • Falla, T.J.; Hancock, R.E. Improved activity of a synthetic indolicidin analog. Antimicrob. Agents Chemother. 1997, 41, 771-775.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 771-775
    • Falla, T.J.1    Hancock, R.E.2
  • 43
    • 0344198180 scopus 로고    scopus 로고
    • Structure-based design of an indolicidin peptide analogue with increased protease stability
    • Rozek, A.; Powers, J.P.; Friedrich, C.L.; Hancock, R.E. Structure-based design of an indolicidin peptide analogue with increased protease stability. Biochemistry 2003, 42, 14130-14138.
    • (2003) Biochemistry , vol.42 , pp. 14130-14138
    • Rozek, A.1    Powers, J.P.2    Friedrich, C.L.3    Hancock, R.E.4
  • 44
    • 0024511945 scopus 로고
    • Determination of the disulfide array in the human defensin hnp-2. A covalently cyclized peptide
    • Selsted, M.E.; Harwig, S.S. Determination of the disulfide array in the human defensin hnp-2. A covalently cyclized peptide. J. Biol. Chem. 1989, 264, 4003-4007.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4003-4007
    • Selsted, M.E.1    Harwig, S.S.2
  • 45
    • 20444387986 scopus 로고    scopus 로고
    • The human cathelicidin ll-37: A multifunctional peptide involved in infection and inflammation in the lung
    • Tjabringa, G.S.; Rabe, K.F.; Hiemstra, P.S. The human cathelicidin ll-37: A multifunctional peptide involved in infection and inflammation in the lung. Pulm. Pharmacol. Ther. 2005, 18, 321-327.
    • (2005) Pulm. Pharmacol. Ther. , vol.18 , pp. 321-327
    • Tjabringa, G.S.1    Rabe, K.F.2    Hiemstra, P.S.3
  • 46
    • 0028263457 scopus 로고
    • Identification of a new member of the protegrin family by cdna cloning
    • Zhao, C.; Liu, L.; Lehrer, R.I. Identification of a new member of the protegrin family by cdna cloning. FEBS Lett. 1994, 346, 285-288.
    • (1994) FEBS Lett. , vol.346 , pp. 285-288
    • Zhao, C.1    Liu, L.2    Lehrer, R.I.3
  • 47
    • 0037501736 scopus 로고    scopus 로고
    • The role of defensins in lung biology and therapy
    • Cole, A.M.; Waring, A.J. The role of defensins in lung biology and therapy. Am. J. Respir. Med. 2002, 1, 249-259.
    • (2002) Am. J. Respir. Med. , vol.1 , pp. 249-259
    • Cole, A.M.1    Waring, A.J.2
  • 48
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from xenopus skin: Isolation, characterization of two active forms, and partial cdna sequence of a precursor
    • Zasloff, M. Magainins, a class of antimicrobial peptides from xenopus skin: Isolation, characterization of two active forms, and partial cdna sequence of a precursor. Proc. Natl. Acad. Sci. USA 1987, 84, 5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 49
    • 0020039463 scopus 로고
    • Secondary structure of the cecropins: Antibacterial peptides from the moth hyalophora cecropia
    • Steiner, H. Secondary structure of the cecropins: Antibacterial peptides from the moth hyalophora cecropia. FEBS Lett. 1982, 137, 283-287.
    • (1982) FEBS Lett. , vol.137 , pp. 283-287
    • Steiner, H.1
  • 50
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • Dempsey, C.E. The actions of melittin on membranes. Biochim. Biophys. Acta 1990, 1031, 143-161.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 51
    • 0024741960 scopus 로고
    • Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin ii, and polyphemusins i and ii: Chemical structures and biological activity
    • Miyata, T.; Tokunaga, F.; Yoneya, T.; Yoshikawa, K.; Iwanaga, S.; Niwa, M.; Takao, T.; Shimonishi, Y. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin ii, and polyphemusins i and ii: Chemical structures and biological activity. J. Biochem. 1989, 106, 663-668.
    • (1989) J. Biochem. , vol.106 , pp. 663-668
    • Miyata, T.1    Tokunaga, F.2    Yoneya, T.3    Yoshikawa, K.4    Iwanaga, S.5    Niwa, M.6    Takao, T.7    Shimonishi, Y.8
  • 52
    • 49449117012 scopus 로고
    • Gramicin s - Origin and mode of action
    • Gause, G.F.; Brazhnikova, M.G. Gramicin s - origin and mode of action. Lancet 1944, 2, 715-716.
    • (1944) Lancet , vol.2 , pp. 715-716
    • Gause, G.F.1    Brazhnikova, M.G.2
  • 53
  • 54
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti, M. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 2004, 75, 39-48.
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 56
    • 21744438757 scopus 로고    scopus 로고
    • Human cathelicidin antimicrobial peptide (camp) gene is a direct target of the vitamin d receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin d3
    • Gombart, A.F.; Borregaard, N.; Koeffler, H.P. Human cathelicidin antimicrobial peptide (camp) gene is a direct target of the vitamin d receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin d3. FASEB J. 2005, 19, 1067-1077.
    • (2005) FASEB J. , vol.19 , pp. 1067-1077
    • Gombart, A.F.1    Borregaard, N.2    Koeffler, H.P.3
  • 57
    • 0642367267 scopus 로고    scopus 로고
    • Current understanding of the function of the nuclear vitamin d receptor in response to its natural and synthetic ligands
    • Carlberg, C. Current understanding of the function of the nuclear vitamin d receptor in response to its natural and synthetic ligands. Recent Results Cancer Res. 2003, 164, 29-42.
    • (2003) Recent Results Cancer Res. , vol.164 , pp. 29-42
    • Carlberg, C.1
  • 58
    • 84876806459 scopus 로고    scopus 로고
    • Curcumin induces human cathelicidin antimicrobial peptide gene expression through a vitamin d receptor-independent pathway
    • Guo, C.; Rosoha, E.; Lowry, M.B.; Borregaard, N.; Gombart, A.F. Curcumin induces human cathelicidin antimicrobial peptide gene expression through a vitamin d receptor-independent pathway. J. Nutr. Biochem. 2012, 24, 754-759.
    • (2012) J. Nutr. Biochem. , vol.24 , pp. 754-759
    • Guo, C.1    Rosoha, E.2    Lowry, M.B.3    Borregaard, N.4    Gombart, A.F.5
  • 62
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide ll-37 is a multifunctional modulator of innate immune responses
    • Scott, M.G.; Davidson, D.J.; Gold, M.R.; Bowdish, D.; Hancock, R.E. The human antimicrobial peptide ll-37 is a multifunctional modulator of innate immune responses. J. Immunol. 2002, 169, 3883-3891.
    • (2002) J. Immunol. , vol.169 , pp. 3883-3891
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3    Bowdish, D.4    Hancock, R.E.5
  • 65
    • 38849088077 scopus 로고    scopus 로고
    • Host defense peptide ll-37, in synergy with inflammatory mediator il-1beta, augments immune responses by multiple pathways
    • Yu, J.; Mookherjee, N.; Wee, K.; Bowdish, D.M.; Pistolic, J.; Li, Y.; Rehaume, L.; Hancock, R.E. Host defense peptide ll-37, in synergy with inflammatory mediator il-1beta, augments immune responses by multiple pathways. J. Immunol. 2007, 179, 7684-7691.
    • (2007) J. Immunol. , vol.179 , pp. 7684-7691
    • Yu, J.1    Mookherjee, N.2    Wee, K.3    Bowdish, D.M.4    Pistolic, J.5    Li, Y.6    Rehaume, L.7    Hancock, R.E.8
  • 66
    • 36148980891 scopus 로고    scopus 로고
    • Cathelicidin ll-37 induces the generation of reactive oxygen species and release of human alpha-defensins from neutrophils
    • Zheng, Y.; Niyonsaba, F.; Ushio, H.; Nagaoka, I.; Ikeda, S.; Okumura, K.; Ogawa, H. Cathelicidin ll-37 induces the generation of reactive oxygen species and release of human alpha-defensins from neutrophils. Br. J. Dermatol. 2007, 157, 1124-1131.
    • (2007) Br. J. Dermatol. , vol.157 , pp. 1124-1131
    • Zheng, Y.1    Niyonsaba, F.2    Ushio, H.3    Nagaoka, I.4    Ikeda, S.5    Okumura, K.6    Ogawa, H.7
  • 67
    • 0032708355 scopus 로고    scopus 로고
    • Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide
    • Bals, R.; Weiner, D.J.; Moscioni, A.D.; Meegalla, R.L.; Wilson, J.M. Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide. Infect. Immun. 1999, 67, 6084-6089.
    • (1999) Infect. Immun. , vol.67 , pp. 6084-6089
    • Bals, R.1    Weiner, D.J.2    Moscioni, A.D.3    Meegalla, R.L.4    Wilson, J.M.5
  • 68
  • 69
    • 77954143033 scopus 로고    scopus 로고
    • Human cathelicidin peptide ll-37 modulates the effects of ifn-gamma on apcs
    • Nijnik, A.; Pistolic, J.; Wyatt, A.; Tam, S.; Hancock, R.E. Human cathelicidin peptide ll-37 modulates the effects of ifn-gamma on apcs. J. Immunol. 2009, 183, 5788-5798.
    • (2009) J. Immunol. , vol.183 , pp. 5788-5798
    • Nijnik, A.1    Pistolic, J.2    Wyatt, A.3    Tam, S.4    Hancock, R.E.5
  • 70
    • 0033022730 scopus 로고    scopus 로고
    • Antimicrobial peptides in insects; structure and function
    • Bulet, P.; Hetru, C.; Dimarcq, J.L.; Hoffmann, D. Antimicrobial peptides in insects; structure and function. Dev. Comp. Immunol. 1999, 23, 329-344.
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 329-344
    • Bulet, P.1    Hetru, C.2    Dimarcq, J.L.3    Hoffmann, D.4
  • 71
    • 11344267777 scopus 로고    scopus 로고
    • Insect antimicrobial peptides: Structures, properties and gene regulation
    • Bulet, P.; Stocklin, R. Insect antimicrobial peptides: Structures, properties and gene regulation. Protein Pept. Lett. 2005, 12, 3-11.
    • (2005) Protein Pept. Lett. , vol.12 , pp. 3-11
    • Bulet, P.1    Stocklin, R.2
  • 73
    • 34447282684 scopus 로고    scopus 로고
    • Melittin: A membrane-active peptide with diverse functions
    • Raghuraman, H.; Chattopadhyay, A. Melittin: A membrane-active peptide with diverse functions. Biosci. Rep. 2007, 27, 189-223.
    • (2007) Biosci. Rep. , vol.27 , pp. 189-223
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 74
    • 0015083727 scopus 로고
    • Haemolytic activity and action on the surface tension of aqueous solutions of synthetic melittins and their derivatives
    • Schroder, E.; Lubke, K.; Lehmann, M.; Beetz, I. Haemolytic activity and action on the surface tension of aqueous solutions of synthetic melittins and their derivatives. Experientia 1971, 27, 764-765.
    • (1971) Experientia , vol.27 , pp. 764-765
    • Schroder, E.1    Lubke, K.2    Lehmann, M.3    Beetz, I.4
  • 75
    • 0025717603 scopus 로고
    • Probing the relationships between the structure and hemolytic activity of melittin with a complete set of leucine substitution analogs
    • Blondelle, S.E.; Houghten, R.A. Probing the relationships between the structure and hemolytic activity of melittin with a complete set of leucine substitution analogs. Peptide Res. 1991, 4, 12-18.
    • (1991) Peptide Res. , vol.4 , pp. 12-18
    • Blondelle, S.E.1    Houghten, R.A.2
  • 76
    • 0025833449 scopus 로고
    • Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin
    • Blondelle, S.E.; Houghten, R.A. Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin. Biochemistry 1991, 30, 4671-4678.
    • (1991) Biochemistry , vol.30 , pp. 4671-4678
    • Blondelle, S.E.1    Houghten, R.A.2
  • 77
    • 77956187583 scopus 로고    scopus 로고
    • Design, recombinant expression, and antibacterial activity of the cecropins-melittin hybrid antimicrobial peptides
    • Cao, Y.; Yu, R.Q.; Liu, Y.; Zhou, H.X.; Song, L.L.; Qiao, D.R. Design, recombinant expression, and antibacterial activity of the cecropins-melittin hybrid antimicrobial peptides. Curr. Microbiol. 2010, 61, 169-175.
    • (2010) Curr. Microbiol. , vol.61 , pp. 169-175
    • Cao, Y.1    Yu, R.Q.2    Liu, Y.3    Zhou, H.X.4    Song, L.L.5    Qiao, D.R.6
  • 78
    • 84908371144 scopus 로고    scopus 로고
    • Cecropin a-melittin mutant with improved proteolytic stability and enhanced antimicrobial activity against bacteria and fungi associated with gastroenteritis in vitro
    • Ji, S.; Li, W.; Zhang, L.; Zhang, Y.; Cao, B. Cecropin a-melittin mutant with improved proteolytic stability and enhanced antimicrobial activity against bacteria and fungi associated with gastroenteritis in vitro. Biochem. Biophys. Res. Commun. 2014, 451, 650-655.
    • (2014) Biochem. Biophys. Res. Commun. , vol.451 , pp. 650-655
    • Ji, S.1    Li, W.2    Zhang, L.3    Zhang, Y.4    Cao, B.5
  • 79
    • 33846490889 scopus 로고    scopus 로고
    • Plant lipid binding proteins: Properties and applications
    • Marion, D.; Bakan, B.; Elmorjani, K. Plant lipid binding proteins: Properties and applications. Biotechnol. Adv. 2007, 25, 195-197.
    • (2007) Biotechnol. Adv. , vol.25 , pp. 195-197
    • Marion, D.1    Bakan, B.2    Elmorjani, K.3
  • 80
    • 77954043686 scopus 로고    scopus 로고
    • Plant defensins: Defense, development and application
    • Stotz, H.U.; Thomson, J.G.; Wang, Y. Plant defensins: Defense, development and application. Plant Signal. Behav. 2009, 4, 1010-1012.
    • (2009) Plant Signal. Behav. , vol.4 , pp. 1010-1012
    • Stotz, H.U.1    Thomson, J.G.2    Wang, Y.3
  • 81
    • 0027969049 scopus 로고
    • Structural features of plant chitinases and chitin-binding proteins
    • Beintema, J.J. Structural features of plant chitinases and chitin-binding proteins. FEBS Lett. 1994, 350, 159-163.
    • (1994) FEBS Lett. , vol.350 , pp. 159-163
    • Beintema, J.J.1
  • 82
    • 84897372103 scopus 로고    scopus 로고
    • Chemistry and biology of cyclotides: Circular plant peptides outside the box
    • Burman, R.; Gunasekera, S.; Stromstedt, A.A.; Goransson, U. Chemistry and biology of cyclotides: Circular plant peptides outside the box. J. Nat. Prod. 2014, 77, 724-736.
    • (2014) J. Nat. Prod. , vol.77 , pp. 724-736
    • Burman, R.1    Gunasekera, S.2    Stromstedt, A.A.3    Goransson, U.4
  • 83
    • 33745304784 scopus 로고    scopus 로고
    • Plant thionins--the structural perspective
    • Stec, B. Plant thionins--the structural perspective. Cell. Mol. Life Sci. 2006, 63, 1370-1385.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 1370-1385
    • Stec, B.1
  • 84
    • 80053245941 scopus 로고    scopus 로고
    • Lipid binding interactions of antimicrobial plant seed defence proteins: Puroindoline-a and beta-purothionin
    • Clifton, L.A.; Sanders, M.R.; Hughes, A.V.; Neylon, C.; Frazier, R.A.; Green, R.J. Lipid binding interactions of antimicrobial plant seed defence proteins: Puroindoline-a and beta-purothionin. Phys. Chem. Chem. Physics 2011, 13, 17153-17162.
    • (2011) Phys. Chem. Chem. Physics , vol.13 , pp. 17153-17162
    • Clifton, L.A.1    Sanders, M.R.2    Hughes, A.V.3    Neylon, C.4    Frazier, R.A.5    Green, R.J.6
  • 85
    • 0016233180 scopus 로고
    • Isolation and characterization of viscotoxin 1-ps from viscum album l. Ssp. Austriacum (wiesb.) vollmann, growing on pinus silvestris
    • Samuelsson, G.; Jayawardene, A.L. Isolation and characterization of viscotoxin 1-ps from viscum album l. Ssp. Austriacum (wiesb.) vollmann, growing on pinus silvestris. Acta Pharm. Suec. 1974, 11, 175-184.
    • (1974) Acta Pharm. Suec. , vol.11 , pp. 175-184
    • Samuelsson, G.1    Jayawardene, A.L.2
  • 86
    • 0041843711 scopus 로고    scopus 로고
    • Interaction of viscotoxins a3 and b with membrane model systems: Implications to their mechanism of action
    • Giudici, M.; Pascual, R.; de la Canal, L.; Pfuller, K.; Pfuller, U.; Villalain, J. Interaction of viscotoxins a3 and b with membrane model systems: Implications to their mechanism of action. Biophys. J. 2003, 85, 971-981.
    • (2003) Biophys. J. , vol.85 , pp. 971-981
    • Giudici, M.1    Pascual, R.2    de la Canal, L.3    Pfuller, K.4    Pfuller, U.5    Villalain, J.6
  • 87
    • 0029199404 scopus 로고
    • Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 2: Structure of beta-purothionin at 1.7 a resolution
    • Stec, B.; Rao, U.; Teeter, M.M. Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 2: Structure of beta-purothionin at 1.7 a resolution. Acta Crystallogr. D Biol. Crystallogr. 1995, 51, 914-924.
    • (1995) Acta Crystallogr. D Biol. Crystallogr. , vol.51 , pp. 914-924
    • Stec, B.1    Rao, U.2    Teeter, M.M.3
  • 88
    • 0027395308 scopus 로고
    • Solution structure of gamma 1-h and gamma 1-p thionins from barley and wheat endosperm determined by 1h-nmr: A structural motif common to toxic arthropod proteins
    • Bruix, M.; Jimenez, M.A.; Santoro, J.; Gonzalez, C.; Colilla, F.J.; Mendez, E.; Rico, M. Solution structure of gamma 1-h and gamma 1-p thionins from barley and wheat endosperm determined by 1h-nmr: A structural motif common to toxic arthropod proteins. Biochemistry 1993, 32, 715-724.
    • (1993) Biochemistry , vol.32 , pp. 715-724
    • Bruix, M.1    Jimenez, M.A.2    Santoro, J.3    Gonzalez, C.4    Colilla, F.J.5    Mendez, E.6    Rico, M.7
  • 89
    • 0242600549 scopus 로고    scopus 로고
    • Structural characterization of hellethionins from helleborus purpurascens
    • Milbradt, A.G.; Kerek, F.; Moroder, L.; Renner, C. Structural characterization of hellethionins from helleborus purpurascens. Biochemistry 2003, 42, 2404-2411.
    • (2003) Biochemistry , vol.42 , pp. 2404-2411
    • Milbradt, A.G.1    Kerek, F.2    Moroder, L.3    Renner, C.4
  • 90
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter, P.D.; Hill, C.; Ross, R.P. Bacteriocins: Developing innate immunity for food. Nat. Rev. Microbiol. 2005, 3, 777-788.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 91
    • 0001198495 scopus 로고
    • The inhibiting effect of streptococcus lactis on lactobacillus bulgaricus
    • Rogers, L.A. The inhibiting effect of streptococcus lactis on lactobacillus bulgaricus. J. Bacteriol. 1928, 16, 321-325.
    • (1928) J. Bacteriol. , vol.16 , pp. 321-325
    • Rogers, L.A.1
  • 92
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid ii combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann, I.; Breukink, E.; van Kraaij, C.; Kuipers, O.P.; Bierbaum, G.; de Kruijff, B.; Sahl, H.G. Specific binding of nisin to the peptidoglycan precursor lipid ii combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. J. Biol. Chem. 2001, 276, 1772-1779.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    van Kraaij, C.3    Kuipers, O.P.4    Bierbaum, G.5    de Kruijff, B.6    Sahl, H.G.7
  • 93
    • 4444277132 scopus 로고    scopus 로고
    • Assembly and stability of nisin-lipid ii pores
    • Hasper, H.E.; de Kruijff, B.; Breukink, E. Assembly and stability of nisin-lipid ii pores. Biochemistry 2004, 43, 11567-11575.
    • (2004) Biochemistry , vol.43 , pp. 11567-11575
    • Hasper, H.E.1    de Kruijff, B.2    Breukink, E.3
  • 94
    • 0034702860 scopus 로고    scopus 로고
    • Binding of nisin z to bilayer vesicles as determined with isothermal titration calorimetry
    • Breukink, E.; Ganz, P.; de Kruijff, B.; Seelig, J. Binding of nisin z to bilayer vesicles as determined with isothermal titration calorimetry. Biochemistry 2000, 39, 10247-10254.
    • (2000) Biochemistry , vol.39 , pp. 10247-10254
    • Breukink, E.1    Ganz, P.2    de Kruijff, B.3    Seelig, J.4
  • 96
    • 0030597972 scopus 로고    scopus 로고
    • Structure-activity relationships in the peptide antibiotic nisin: Antibacterial activity of fragments of nisin
    • Chan, W.C.; Leyland, M.; Clark, J.; Dodd, H.M.; Lian, L.Y.; Gasson, M.J.; Bycroft, B.W.; Roberts, G.C. Structure-activity relationships in the peptide antibiotic nisin: Antibacterial activity of fragments of nisin. FEBS Lett. 1996, 390, 129-132.
    • (1996) FEBS Lett. , vol.390 , pp. 129-132
    • Chan, W.C.1    Leyland, M.2    Clark, J.3    Dodd, H.M.4    Lian, L.Y.5    Gasson, M.J.6    Bycroft, B.W.7    Roberts, G.C.8
  • 97
    • 0034666332 scopus 로고    scopus 로고
    • Covalent attachment of oligodeoxyribonucleotides to amine-modified si (001) surfaces
    • Strother, T.; Hamers, R.J.; Smith, L.M. Covalent attachment of oligodeoxyribonucleotides to amine-modified si (001) surfaces. Nucleic Acids Res. 2000, 28, 3535-3541.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3535-3541
    • Strother, T.1    Hamers, R.J.2    Smith, L.M.3
  • 99
    • 84877318780 scopus 로고    scopus 로고
    • Antimicrobial peptides stage a comeback
    • Fox, J.L. Antimicrobial peptides stage a comeback. Nat. Biotechnol. 2013, 31, 379-382.
    • (2013) Nat. Biotechnol. , vol.31 , pp. 379-382
    • Fox, J.L.1
  • 100
    • 84929051849 scopus 로고    scopus 로고
    • Recombinant lysostaphin protects mice from methicillin-resistant staphylococcus aureus pneumonia
    • Chen, C.; Fan, H.; Huang, Y.; Peng, F.; Yuan, S.; Tong, Y. Recombinant lysostaphin protects mice from methicillin-resistant staphylococcus aureus pneumonia. BioMed Res. Int. 2014, 2014, 602185.
    • (2014) BioMed Res. Int. , vol.2014
    • Chen, C.1    Fan, H.2    Huang, Y.3    Peng, F.4    Yuan, S.5    Tong, Y.6
  • 101
    • 0025903814 scopus 로고
    • Crystal structure of defensin hnp-3, an amphiphilic dimer: Mechanisms of membrane permeabilization
    • Hill, C.P.; Yee, J.; Selsted, M.E.; Eisenberg, D. Crystal structure of defensin hnp-3, an amphiphilic dimer: Mechanisms of membrane permeabilization. Science 1991, 251, 1481-1485.
    • (1991) Science , vol.251 , pp. 1481-1485
    • Hill, C.P.1    Yee, J.2    Selsted, M.E.3    Eisenberg, D.4
  • 102
    • 0026490907 scopus 로고
    • Nmr studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit np-2 and human hnp-1
    • Zhang, X.L.; Selsted, M.E.; Pardi, A. Nmr studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit np-2 and human hnp-1. Biochemistry 1992, 31, 11348-11356.
    • (1992) Biochemistry , vol.31 , pp. 11348-11356
    • Zhang, X.L.1    Selsted, M.E.2    Pardi, A.3
  • 103
    • 0026468973 scopus 로고
    • Nmr studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit np-2 and human hnp-1
    • Pardi, A.; Zhang, X.L.; Selsted, M.E.; Skalicky, J.J.; Yip, P.F. Nmr studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit np-2 and human hnp-1. Biochemistry 1992, 31, 11357-11364.
    • (1992) Biochemistry , vol.31 , pp. 11357-11364
    • Pardi, A.1    Zhang, X.L.2    Selsted, M.E.3    Skalicky, J.J.4    Yip, P.F.5
  • 104
    • 77951271759 scopus 로고    scopus 로고
    • Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid ii
    • De Leeuw, E.; Li, C.; Zeng, P.; Diepeveen-de Buin, M.; Lu, W.Y.; Breukink, E.; Lu, W. Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid ii. FEBS Lett. 2010, 584, 1543-1548.
    • (2010) FEBS Lett. , vol.584 , pp. 1543-1548
    • De Leeuw, E.1    Li, C.2    Zeng, P.3    Diepeveen-De Buin, M.4    Lu, W.Y.5    Breukink, E.6    Lu, W.7
  • 105
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, M.R.; Yount, N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 2003, 55, 27-55.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 106
    • 0029146071 scopus 로고
    • Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides
    • Epand, R.M.; Shai, Y.; Segrest, J.P.; Anantharamaiah, G.M. Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides. Biopolymers 1995, 37, 319-338.
    • (1995) Biopolymers , vol.37 , pp. 319-338
    • Epand, R.M.1    Shai, Y.2    Segrest, J.P.3    Anantharamaiah, G.M.4
  • 107
    • 84866943640 scopus 로고    scopus 로고
    • Antimicrobial activity of peptidomimetics against multidrug-resistant escherichia coli : A comparative study of different backbones
    • Jahnsen, R.D.; Frimodt-Moller, N.; Franzyk, H. Antimicrobial activity of peptidomimetics against multidrug-resistant escherichia coli : A comparative study of different backbones. J. Med. Chem. 2012, 55, 7253-7261.
    • (2012) J. Med. Chem. , vol.55 , pp. 7253-7261
    • Jahnsen, R.D.1    Frimodt-Moller, N.2    Franzyk, H.3
  • 108
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R.M.; Vogel, H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1999, 1462, 11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 109
    • 0029870910 scopus 로고    scopus 로고
    • Helix propensities of basic amino acids increase with the length of the side-chain
    • Padmanabhan, S.; York, E.J.; Stewart, J.M.; Baldwin, R.L. Helix propensities of basic amino acids increase with the length of the side-chain. J. Mol. Biol. 1996, 257, 726-734.
    • (1996) J. Mol. Biol. , vol.257 , pp. 726-734
    • Padmanabhan, S.1    York, E.J.2    Stewart, J.M.3    Baldwin, R.L.4
  • 110
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace, C.N.; Scholtz, J.M. A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 1998, 75, 422-427.
    • (1998) Biophys. J. , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 113
    • 52049114697 scopus 로고    scopus 로고
    • The conserved salt bridge in human alpha-defensin 5 is required for its precursor processing and proteolytic stability
    • Rajabi, M.; de Leeuw, E.; Pazgier, M.; Li, J.; Lubkowski, J.; Lu, W. The conserved salt bridge in human alpha-defensin 5 is required for its precursor processing and proteolytic stability. J. Biol. Chem. 2008, 283, 21509-21518.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21509-21518
    • Rajabi, M.1    de Leeuw, E.2    Pazgier, M.3    Li, J.4    Lubkowski, J.5    Lu, W.6
  • 114
    • 23044463641 scopus 로고    scopus 로고
    • Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent
    • Hunter, H.N.; Demcoe, A.R.; Jenssen, H.; Gutteberg, T.J.; Vogel, H.J. Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent. Antimicrob. Agents Chemother. 2005, 49, 3387-3395.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3387-3395
    • Hunter, H.N.1    Demcoe, A.R.2    Jenssen, H.3    Gutteberg, T.J.4    Vogel, H.J.5
  • 115
    • 84870531632 scopus 로고    scopus 로고
    • Nmr solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5
    • Wommack, A.J.; Robson, S.A.; Wanniarachchi, Y.A.; Wan, A.; Turner, C.J.; Wagner, G.; Nolan, E.M. Nmr solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5. Biochemistry 2012, 51, 9624-9637.
    • (2012) Biochemistry , vol.51 , pp. 9624-9637
    • Wommack, A.J.1    Robson, S.A.2    Wanniarachchi, Y.A.3    Wan, A.4    Turner, C.J.5    Wagner, G.6    Nolan, E.M.7
  • 116
    • 67849115958 scopus 로고    scopus 로고
    • Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5
    • De Leeuw, E.; Rajabi, M.; Zou, G.; Pazgier, M.; Lu, W. Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5. FEBS Lett. 2009, 583, 2507-2512.
    • (2009) FEBS Lett. , vol.583 , pp. 2507-2512
    • De Leeuw, E.1    Rajabi, M.2    Zou, G.3    Pazgier, M.4    Lu, W.5
  • 118
    • 33847298627 scopus 로고    scopus 로고
    • Studies of the biological properties of human beta-defensin 1
    • Pazgier, M.; Prahl, A.; Hoover, D.M.; Lubkowski, J. Studies of the biological properties of human beta-defensin 1. J. Biol. Chem. 2007, 282, 1819-1829.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1819-1829
    • Pazgier, M.1    Prahl, A.2    Hoover, D.M.3    Lubkowski, J.4
  • 120
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of hbd3 against staphylococcus aureus
    • Schibli, D.J.; Hunter, H.N.; Aseyev, V.; Starner, T.D.; Wiencek, J.M.; McCray, P.B.; Tack, B.F.; Vogel, H.J. The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of hbd3 against staphylococcus aureus. J. Biol. Chem. 2002, 277, 8279-8289.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray, P.B.6    Tack, B.F.7    Vogel, H.J.8
  • 121
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • Dathe, M.; Nikolenko, H.; Meyer, J.; Beyermann, M.; Bienert, M. Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Lett. 2001, 501, 146-150.
    • (2001) FEBS Lett. , vol.501 , pp. 146-150
    • Dathe, M.1    Nikolenko, H.2    Meyer, J.3    Beyermann, M.4    Bienert, M.5
  • 123
    • 0023848271 scopus 로고
    • Interaction of macrophage cationic proteins with the outer-membrane of pseudomonas-aeruginosa
    • Sawyer, J.G.; Martin, N.L.; Hancock, R.E.W. Interaction of macrophage cationic proteins with the outer-membrane of pseudomonas-aeruginosa. Infect. Immun. 1988, 56, 693-698.
    • (1988) Infect. Immun. , vol.56 , pp. 693-698
    • Sawyer, J.G.1    Martin, N.L.2    Hancock, R.E.W.3
  • 124
    • 0028361454 scopus 로고
    • The interaction of a recombinant cecropin/melittin hybrid peptide with the outer-membrane of pseudomonas-aeruginosa
    • Piers, K.L.; Hancock, R.E.W. The interaction of a recombinant cecropin/melittin hybrid peptide with the outer-membrane of pseudomonas-aeruginosa. Mol. Microbiol. 1994, 12, 951-958.
    • (1994) Mol. Microbiol. , vol.12 , pp. 951-958
    • Piers, K.L.1    Hancock, R.E.W.2
  • 125
    • 67649256037 scopus 로고    scopus 로고
    • Control of cell selectivity of antimicrobial peptides
    • Matsuzaki, K. Control of cell selectivity of antimicrobial peptides. Biochim. Biophys. Acta 2009, 1788, 1687-1692.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1687-1692
    • Matsuzaki, K.1
  • 126
    • 84863230302 scopus 로고    scopus 로고
    • Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions
    • Yin, L.M.; Edwards, M.A.; Li, J.; Yip, C.M.; Deber, C.M. Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions. J. Biol. Chem. 2012, 287, 7738-7745.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7738-7745
    • Yin, L.M.1    Edwards, M.A.2    Li, J.3    Yip, C.M.4    Deber, C.M.5
  • 127
    • 0030664760 scopus 로고    scopus 로고
    • Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment
    • Wieprecht, T.; Dathe, M.; Krause, E.; Beyermann, M.; Maloy, W.L.; MacDonald, D.L.; Bienert, M. Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment. FEBS Lett. 1997, 417, 135-140.
    • (1997) FEBS Lett. , vol.417 , pp. 135-140
    • Wieprecht, T.1    Dathe, M.2    Krause, E.3    Beyermann, M.4    Maloy, W.L.5    McDonald, D.L.6    Bienert, M.7
  • 128
    • 84877287392 scopus 로고    scopus 로고
    • Effect of repetitive lysine-tryptophan motifs on the bactericidal activity of antimicrobial peptides
    • Gopal, R.; Seo, C.H.; Song, P.I.; Park, Y. Effect of repetitive lysine-tryptophan motifs on the bactericidal activity of antimicrobial peptides. Amino acids 2013, 44, 645-660.
    • (2013) Amino acids , vol.44 , pp. 645-660
    • Gopal, R.1    Seo, C.H.2    Song, P.I.3    Park, Y.4
  • 129
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg, D. Three-dimensional structure of membrane and surface proteins. Ann. Rev. Biochem. 1984, 53, 595-623.
    • (1984) Ann. Rev. Biochem. , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 130
    • 34250195381 scopus 로고    scopus 로고
    • Folding amphipathic helices into membranes: Amphiphilicity trumps hydrophobicity
    • Fernandez-Vidall, M.; Jayasinghe, S.; Ladokhin, A.S.; White, S.H. Folding amphipathic helices into membranes: Amphiphilicity trumps hydrophobicity. J. Mol. Biol. 2007, 370, 459-470.
    • (2007) J. Mol. Biol. , vol.370 , pp. 459-470
    • Fernandez-Vidall, M.1    Jayasinghe, S.2    Ladokhin, A.S.3    White, S.H.4
  • 131
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen, Y.; Mant, C.T.; Farmer, S.W.; Hancock, R.E.; Vasil, M.L.; Hodges, R.S. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J. Biol. Chem. 2005, 280, 12316-12329.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 132
    • 84877702474 scopus 로고    scopus 로고
    • Role of amphiphilicity in the design of synthetic mimics of antimicrobial peptides with gram-negative activity
    • Thaker, H.D.; Cankaya, A.; Scott, R.W.; Tew, G.N. Role of amphiphilicity in the design of synthetic mimics of antimicrobial peptides with gram-negative activity. ACS Med. Chem. Lett. 2013, 4, 481-485.
    • (2013) ACS Med. Chem. Lett. , vol.4 , pp. 481-485
    • Thaker, H.D.1    Cankaya, A.2    Scott, R.W.3    Tew, G.N.4
  • 133
    • 4744374646 scopus 로고    scopus 로고
    • Antimicrobial activity of arginine- and tryptophan-rich hexapeptides: The effects of aromatic clusters, d-amino acid substitution and cyclization
    • Wessolowski, A.; Bienert, M.; Dathe, M. Antimicrobial activity of arginine- and tryptophan-rich hexapeptides: The effects of aromatic clusters, d-amino acid substitution and cyclization. J. Pept. Res. 2004, 64, 159-169.
    • (2004) J. Pept. Res. , vol.64 , pp. 159-169
    • Wessolowski, A.1    Bienert, M.2    Dathe, M.3
  • 134
    • 0029069628 scopus 로고
    • Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides
    • Pathak, N.; Salas-Auvert, R.; Ruche, G.; Janna, M.H.; McCarthy, D.; Harrison, R.G. Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides. Proteins 1995, 22, 182-186.
    • (1995) Proteins , vol.22 , pp. 182-186
    • Pathak, N.1    Salas-Auvert, R.2    Ruche, G.3    Janna, M.H.4    McCarthy, D.5    Harrison, R.G.6
  • 135
    • 0026570489 scopus 로고
    • Shortened cecropin a-melittin hybrids. Significant size reduction retains potent antibiotic activity
    • Andreu, D.; Ubach, J.; Boman, A.; Wahlin, B.; Wade, D.; Merrifield, R.B.; Boman, H.G. Shortened cecropin a-melittin hybrids. Significant size reduction retains potent antibiotic activity. FEBS Lett. 1992, 296, 190-194.
    • (1992) FEBS Lett. , vol.296 , pp. 190-194
    • Andreu, D.1    Ubach, J.2    Boman, A.3    Wahlin, B.4    Wade, D.5    Merrifield, R.B.6    Boman, H.G.7
  • 136
    • 0033532175 scopus 로고    scopus 로고
    • Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity
    • Kondejewski, L.H.; Jelokhani-Niaraki, M.; Farmer, S.W.; Lix, B.; Kay, C.M.; Sykes, B.D.; Hancock, R.E.W.; Hodges, R.S. Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity. J. Biol. Chem. 1999, 274, 13181-13192.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13181-13192
    • Kondejewski, L.H.1    Jelokhani-Niaraki, M.2    Farmer, S.W.3    Lix, B.4    Kay, C.M.5    Sykes, B.D.6    Hancock, R.E.W.7    Hodges, R.S.8
  • 138
    • 0030198873 scopus 로고    scopus 로고
    • Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes
    • Fahrner, R.L.; Dieckmann, T.; Harwig, S.S.; Lehrer, R.I.; Eisenberg, D.; Feigon, J. Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes. Chem. Biol. 1996, 3, 543-550.
    • (1996) Chem. Biol. , vol.3 , pp. 543-550
    • Fahrner, R.L.1    Dieckmann, T.2    Harwig, S.S.3    Lehrer, R.I.4    Eisenberg, D.5    Feigon, J.6
  • 139
    • 78751687696 scopus 로고    scopus 로고
    • Interaction of w-substituted analogs of cyclo-rrrwfw with bacterial lipopolysaccharides: The role of the aromatic cluster in antimicrobial activity
    • Bagheri, M.; Keller, S.; Dathe, M. Interaction of w-substituted analogs of cyclo-rrrwfw with bacterial lipopolysaccharides: The role of the aromatic cluster in antimicrobial activity. Antimicrob. Agents Chemother. 2011, 55, 788-797.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 788-797
    • Bagheri, M.1    Keller, S.2    Dathe, M.3
  • 140
    • 84884409922 scopus 로고    scopus 로고
    • What goes around comes around-a comparative study of the influence of chemical modifications on the antimicrobial properties of small cyclic peptides
    • Scheinpflug, K.; Nikolenko, H.; Komarov, I.V.; Rautenbach, M.; Dathe, M. What goes around comes around-a comparative study of the influence of chemical modifications on the antimicrobial properties of small cyclic peptides. Pharmaceuticals (Basel) 2013, 6, 1130-1144.
    • (2013) Pharmaceuticals (Basel) , vol.6 , pp. 1130-1144
    • Scheinpflug, K.1    Nikolenko, H.2    Komarov, I.V.3    Rautenbach, M.4    Dathe, M.5
  • 142
    • 0029816946 scopus 로고    scopus 로고
    • Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin s analogs
    • Kondejewski, L.H.; Farmer, S.W.; Wishart, D.S.; Kay, C.M.; Hancock, R.E.; Hodges, R.S. Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin s analogs. J. Biol. Chem. 1996, 271, 25261-25268.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25261-25268
    • Kondejewski, L.H.1    Farmer, S.W.2    Wishart, D.S.3    Kay, C.M.4    Hancock, R.E.5    Hodges, R.S.6
  • 143
    • 24744466153 scopus 로고    scopus 로고
    • Structure of the antimicrobial, cationic hexapeptide cyclo(rrwwrf) and its analogues in solution and bound to detergent micelles
    • Appelt, C.; Wessolowski, A.; Soderhall, J.A.; Dathe, M.; Schmieder, P. Structure of the antimicrobial, cationic hexapeptide cyclo(rrwwrf) and its analogues in solution and bound to detergent micelles. Chembiochem 2005, 6, 1654-1662.
    • (2005) Chembiochem , vol.6 , pp. 1654-1662
    • Appelt, C.1    Wessolowski, A.2    Soderhall, J.A.3    Dathe, M.4    Schmieder, P.5
  • 144
    • 0036495674 scopus 로고    scopus 로고
    • Circular proteins--no end in sight
    • Trabi, M.; Craik, D.J. Circular proteins--no end in sight. Trends Biochem. Sci. 2002, 27, 132-138.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 132-138
    • Trabi, M.1    Craik, D.J.2
  • 148
    • 84861123585 scopus 로고    scopus 로고
    • Strand length-dependent antimicrobial activity and membrane-active mechanism of arginine- and valine-rich beta-hairpin-like antimicrobial peptides
    • Dong, N.; Ma, Q.; Shan, A.; Lv, Y.; Hu, W.; Gu, Y.; Li, Y. Strand length-dependent antimicrobial activity and membrane-active mechanism of arginine- and valine-rich beta-hairpin-like antimicrobial peptides. Antimicrob. Agents Chemother. 2012, 56, 2994-3003.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 2994-3003
    • Dong, N.1    Ma, Q.2    Shan, A.3    Lv, Y.4    Hu, W.5    Gu, Y.6    Li, Y.7
  • 149
    • 84903701599 scopus 로고    scopus 로고
    • High-quality 3d structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin ll-37 and its fragments
    • Wang, G.; Mishra, B.; Epand, R.F.; Epand, R.M. High-quality 3d structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin ll-37 and its fragments. Biochim. Biophys. Acta 2014, 1838, 2160-2172.
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 2160-2172
    • Wang, G.1    Mishra, B.2    Epand, R.F.3    Epand, R.M.4
  • 150
  • 151
    • 0043167827 scopus 로고    scopus 로고
    • Molecular dynamics simulations of pentapeptides at interfaces: Salt bridge and cation-pi interactions
    • Aliste, M.P.; MacCallum, J.L.; Tieleman, D.P. Molecular dynamics simulations of pentapeptides at interfaces: Salt bridge and cation-pi interactions. Biochemistry 2003, 42, 8976-8987.
    • (2003) Biochemistry , vol.42 , pp. 8976-8987
    • Aliste, M.P.1    McCallum, J.L.2    Tieleman, D.P.3
  • 153
    • 0029860472 scopus 로고    scopus 로고
    • Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin
    • Kang, J.H.; Lee, M.K.; Kim, K.L.; Hahm, K.S. Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin. Int. J. Pept. Protein Res. 1996, 48, 357-363.
    • (1996) Int. J. Pept. Protein Res. , vol.48 , pp. 357-363
    • Kang, J.H.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.S.4
  • 154
    • 70349639934 scopus 로고    scopus 로고
    • Effect of leucine and lysine substitution on the antimicrobial activity and evaluation of the mechanism of the hpa3nt3 analog peptide
    • Gopal, R.; Park, S.C.; Ha, K.J.; Cho, S.J.; Kim, S.W.; Song, P.I.; Nah, J.W.; Park, Y.; Hahm, K.S. Effect of leucine and lysine substitution on the antimicrobial activity and evaluation of the mechanism of the hpa3nt3 analog peptide. J. Pept. Sci. 2009, 15, 589-594.
    • (2009) J. Pept. Sci. , vol.15 , pp. 589-594
    • Gopal, R.1    Park, S.C.2    Ha, K.J.3    Cho, S.J.4    Kim, S.W.5    Song, P.I.6    Nah, J.W.7    Park, Y.8    Hahm, K.S.9
  • 155
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • Mitchell, D.J.; Kim, D.T.; Steinman, L.; Fathman, C.G.; Rothbard, J.B. Polyarginine enters cells more efficiently than other polycationic homopolymers. J. Pept. Res. 2000, 56, 318-325.
    • (2000) J. Pept. Res. , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Steinman, L.3    Fathman, C.G.4    Rothbard, J.B.5
  • 157
    • 84883096593 scopus 로고    scopus 로고
    • Differential mode of antimicrobial actions of arginine-rich and lysine-rich histones against gram-positive staphylococcus aureus
    • Morita, S.; Tagai, C.; Shiraishi, T.; Miyaji, K.; Iwamuro, S. Differential mode of antimicrobial actions of arginine-rich and lysine-rich histones against gram-positive staphylococcus aureus. Peptides 2013, 48, 75-82.
    • (2013) Peptides , vol.48 , pp. 75-82
    • Morita, S.1    Tagai, C.2    Shiraishi, T.3    Miyaji, K.4    Iwamuro, S.5
  • 158
    • 55349100857 scopus 로고    scopus 로고
    • Antimicrobial action of histone h2b in escherichia coli: Evidence for membrane translocation and DNA-binding of a histone h2b fragment after proteolytic cleavage by outer membrane proteinase t
    • Kawasaki, H.; Koyama, T.; Conlon, J.M.; Yamakura, F.; Iwamuro, S. Antimicrobial action of histone h2b in escherichia coli: Evidence for membrane translocation and DNA-binding of a histone h2b fragment after proteolytic cleavage by outer membrane proteinase t. Biochimie 2008, 90, 1693-1702.
    • (2008) Biochimie , vol.90 , pp. 1693-1702
    • Kawasaki, H.1    Koyama, T.2    Conlon, J.M.3    Yamakura, F.4    Iwamuro, S.5
  • 159
    • 80054064119 scopus 로고    scopus 로고
    • Antimicrobial properties of arginineand lysine-rich histones and involvement of bacterial outer membrane protease t in their differential mode of actions
    • Tagai, C.; Morita, S.; Shiraishi, T.; Miyaji, K.; Iwamuro, S. Antimicrobial properties of arginineand lysine-rich histones and involvement of bacterial outer membrane protease t in their differential mode of actions. Peptides 2011, 32, 2003-2009.
    • (2011) Peptides , vol.32 , pp. 2003-2009
    • Tagai, C.1    Morita, S.2    Shiraishi, T.3    Miyaji, K.4    Iwamuro, S.5
  • 160
    • 84876305449 scopus 로고    scopus 로고
    • Biomolecular engineering of a human beta defensin model for increased salt resistance
    • Li, X.; Saravanan, R.; Kwak, S.K.; Leong, S.S.J. Biomolecular engineering of a human beta defensin model for increased salt resistance. Chem. Eng. Sci. 2013, 95, 128-137.
    • (2013) Chem. Eng. Sci. , vol.95 , pp. 128-137
    • Li, X.1    Saravanan, R.2    Kwak, S.K.3    Leong, S.S.J.4
  • 162
    • 36849039966 scopus 로고    scopus 로고
    • Tuning the membrane selectivity of antimicrobial peptides by using multivalent design
    • Liu, Z.; Young, A.W.; Hu, P.; Rice, A.J.; Zhou, C.; Zhang, Y.; Kallenbach, N.R. Tuning the membrane selectivity of antimicrobial peptides by using multivalent design. Chembiochem 2007, 8, 2063-2065.
    • (2007) Chembiochem , vol.8 , pp. 2063-2065
    • Liu, Z.1    Young, A.W.2    Hu, P.3    Rice, A.J.4    Zhou, C.5    Zhang, Y.6    Kallenbach, N.R.7
  • 163
    • 84867497967 scopus 로고    scopus 로고
    • Transformation of an antimicrobial peptide into a plasma membrane-permeable, mitochondria-targeted peptide via the substitution of lysine with arginine
    • Nakase, I.; Okumura, S.; Katayama, S.; Hirose, H.; Pujals, S.; Yamaguchi, H.; Arakawa, S.; Shimizu, S.; Futaki, S. Transformation of an antimicrobial peptide into a plasma membrane-permeable, mitochondria-targeted peptide via the substitution of lysine with arginine. Chem. Commun. (Camb) 2012, 48, 11097-11099.
    • (2012) Chem. Commun. (Camb) , vol.48 , pp. 11097-11099
    • Nakase, I.1    Okumura, S.2    Katayama, S.3    Hirose, H.4    Pujals, S.5    Yamaguchi, H.6    Arakawa, S.7    Shimizu, S.8    Futaki, S.9
  • 164
    • 0036185339 scopus 로고    scopus 로고
    • Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides
    • Vogel, H.J.; Schibli, D.J.; Jing, W.; Lohmeier-Vogel, E.M.; Epand, R.F.; Epand, R.M. Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides. Biochem. Cell Biol. 2002, 80, 49-63.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 49-63
    • Vogel, H.J.1    Schibli, D.J.2    Jing, W.3    Lohmeier-Vogel, E.M.4    Epand, R.F.5    Epand, R.M.6
  • 165
    • 33847151791 scopus 로고    scopus 로고
    • Cation-pi interactions stabilize the structure of the antimicrobial peptide indolicidin near membranes: Molecular dynamics simulations
    • Khandelia, H.; Kaznessis, Y.N. Cation-pi interactions stabilize the structure of the antimicrobial peptide indolicidin near membranes: Molecular dynamics simulations. J. Phys. Chemi. B 2007, 111, 242-250.
    • (2007) J. Phys. Chemi. B , vol.111 , pp. 242-250
    • Khandelia, H.1    Kaznessis, Y.N.2
  • 166
    • 84901493950 scopus 로고    scopus 로고
    • Antimicrobial properties and interaction of two trp-substituted cationic antimicrobial peptides with a lipid bilayer
    • Bi, X.; Wang, C.; Dong, W.; Zhu, W.; Shang, D. Antimicrobial properties and interaction of two trp-substituted cationic antimicrobial peptides with a lipid bilayer. J. Antibiot. 2014, 67, 361-368.
    • (2014) J. Antibiot. , vol.67 , pp. 361-368
    • Bi, X.1    Wang, C.2    Dong, W.3    Zhu, W.4    Shang, D.5
  • 167
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W.M.; Wimley, W.C.; Gawrisch, K.; White, S.H. The preference of tryptophan for membrane interfaces. Biochemistry 1998, 37, 14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 168
    • 0037443086 scopus 로고    scopus 로고
    • Interactions of the designed antimicrobial peptide mb21 and truncated dermaseptin s3 with lipid bilayers: Molecular-dynamics simulations
    • Shepherd, C.M.; Vogel, H.J.; Tieleman, D.P. Interactions of the designed antimicrobial peptide mb21 and truncated dermaseptin s3 with lipid bilayers: Molecular-dynamics simulations. Biochem. J. 2003, 370, 233-243.
    • (2003) Biochem. J. , vol.370 , pp. 233-243
    • Shepherd, C.M.1    Vogel, H.J.2    Tieleman, D.P.3
  • 169
    • 84881669101 scopus 로고    scopus 로고
    • Investigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action
    • Bi, X.; Wang, C.; Ma, L.; Sun, Y.; Shang, D. Investigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action. J. Appl. Microbiol. 2013, 115, 663-672.
    • (2013) J. Appl. Microbiol. , vol.115 , pp. 663-672
    • Bi, X.1    Wang, C.2    Ma, L.3    Sun, Y.4    Shang, D.5
  • 172
    • 27644584146 scopus 로고    scopus 로고
    • Antibacterial activity of human neutrophil defensin hnp-1 analogs without cysteines
    • Varkey, J.; Nagaraj, R. Antibacterial activity of human neutrophil defensin hnp-1 analogs without cysteines. Antimicrob. Agents Chemother. 2005, 49, 4561-4566.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4561-4566
    • Varkey, J.1    Nagaraj, R.2
  • 173
    • 22244480342 scopus 로고    scopus 로고
    • Structure-activity relation of human beta-defensin 3: Influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity
    • Kluver, E.; Schulz-Maronde, S.; Scheid, S.; Meyer, B.; Forssmann, W.G.; Adermann, K. Structure-activity relation of human beta-defensin 3: Influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity. Biochemistry 2005, 44, 9804-9816.
    • (2005) Biochemistry , vol.44 , pp. 9804-9816
    • Kluver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.G.5    Adermann, K.6
  • 174
    • 0034727645 scopus 로고    scopus 로고
    • Interaction of polyphemusin i and structural analogs with bacterial membranes, lipopolysaccharide, and lipid monolayers
    • Zhang, L.; Scott, M.G.; Yan, H.; Mayer, L.D.; Hancock, R.E. Interaction of polyphemusin i and structural analogs with bacterial membranes, lipopolysaccharide, and lipid monolayers. Biochemistry 2000, 39, 14504-14514.
    • (2000) Biochemistry , vol.39 , pp. 14504-14514
    • Zhang, L.1    Scott, M.G.2    Yan, H.3    Mayer, L.D.4    Hancock, R.E.5
  • 175
    • 11144242839 scopus 로고    scopus 로고
    • Protegrin structure-activity relationships: Using homology models of synthetic sequences to determine structural characteristics important for activity
    • Ostberg, N.; Kaznessis, Y. Protegrin structure-activity relationships: Using homology models of synthetic sequences to determine structural characteristics important for activity. Peptides 2005, 26, 197-206.
    • (2005) Peptides , vol.26 , pp. 197-206
    • Ostberg, N.1    Kaznessis, Y.2
  • 176
    • 50849120027 scopus 로고    scopus 로고
    • Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1
    • Gottler, L.M.; de la Salud Bea, R.; Shelburne, C.E.; Ramamoorthy, A.; Marsh, E.N. Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1. Biochemistry 2008, 47, 9243-9250.
    • (2008) Biochemistry , vol.47 , pp. 9243-9250
    • Gottler, L.M.1    de la Salud Bea, R.2    Shelburne, C.E.3    Ramamoorthy, A.4    Marsh, E.N.5
  • 177
    • 0033858613 scopus 로고    scopus 로고
    • Development of protegrins for the treatment and prevention of oral mucositis: Structure-activity relationships of synthetic protegrin analogues
    • Chen, J.; Falla, T.J.; Liu, H.; Hurst, M.A.; Fujii, C.A.; Mosca, D.A.; Embree, J.R.; Loury, D.J.; Radel, P.A.; Cheng Chang, C.; et al. Development of protegrins for the treatment and prevention of oral mucositis: Structure-activity relationships of synthetic protegrin analogues. Biopolymers 2000, 55, 88-98.
    • (2000) Biopolymers , vol.55 , pp. 88-98
    • Chen, J.1    Falla, T.J.2    Liu, H.3    Hurst, M.A.4    Fujii, C.A.5    Mosca, D.A.6    Embree, J.R.7    Loury, D.J.8    Radel, P.A.9    Cheng Chang, C.10
  • 179
    • 0029831079 scopus 로고    scopus 로고
    • Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations
    • Harwig, S.S.; Waring, A.; Yang, H.J.; Cho, Y.; Tan, L.; Lehrer, R.I. Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations. Eur. J. Biochem. 1996, 240, 352-357.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 352-357
    • Harwig, S.S.1    Waring, A.2    Yang, H.J.3    Cho, Y.4    Tan, L.5    Lehrer, R.I.6
  • 180
    • 84873328552 scopus 로고    scopus 로고
    • Membrane interactions and pore formation by the antimicrobial peptide protegrin
    • Lazaridis, T.; He, Y.; Prieto, L. Membrane interactions and pore formation by the antimicrobial peptide protegrin. Biophys. J. 2013, 104, 633-642.
    • (2013) Biophys. J. , vol.104 , pp. 633-642
    • Lazaridis, T.1    He, Y.2    Prieto, L.3
  • 181
    • 33750820630 scopus 로고    scopus 로고
    • Membrane-dependent oligomeric structure and pore formation of beta-hairpin antimicrobial peptide in lipid bilayers from solid-state nmr
    • Mani, R.; Cady, S.D.; Tang, M.; Waring, A.J.; Lehrert, R.I.; Hong, M. Membrane-dependent oligomeric structure and pore formation of beta-hairpin antimicrobial peptide in lipid bilayers from solid-state nmr. Proc. Natl. Acad. Sci. USA 2006, 103, 16242-16247.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16242-16247
    • Mani, R.1    Cady, S.D.2    Tang, M.3    Waring, A.J.4    Lehrert, R.I.5    Hong, M.6
  • 183
    • 84905843048 scopus 로고    scopus 로고
    • Cysteine deleted protegrin-1 (cdp-1): Anti-bacterial activity, outer-membrane disruption and selectivity
    • Mohanram, H.; Bhattacharjya, S. Cysteine deleted protegrin-1 (cdp-1): Anti-bacterial activity, outer-membrane disruption and selectivity. Biochim. Biophys. Acta 2014, 1840, 3006-3016.
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 3006-3016
    • Mohanram, H.1    Bhattacharjya, S.2
  • 184
    • 0033948397 scopus 로고    scopus 로고
    • Ib-367, a protegrin peptide with in vitro and in vivo activities against the microflora associated with oral mucositis
    • Mosca, D.A.; Hurst, M.A.; So, W.; Viajar, B.S.; Fujii, C.A.; Falla, T.J. Ib-367, a protegrin peptide with in vitro and in vivo activities against the microflora associated with oral mucositis. Antimicrob. Agents Chemother. 2000, 44, 1803-1808.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 1803-1808
    • Mosca, D.A.1    Hurst, M.A.2    So, W.3    Viajar, B.S.4    Fujii, C.A.5    Falla, T.J.6
  • 185
    • 10744229987 scopus 로고    scopus 로고
    • A multinational, randomized phase iii trial of iseganan hcl oral solution for reducing the severity of oral mucositis in patients receiving radiotherapy for head-andneck malignancy
    • Trotti, A.; Garden, A.; Warde, P.; Symonds, P.; Langer, C.; Redman, R.; Pajak, T.F.; Fleming, T.R.; Henke, M.; Bourhis, J.; et al. A multinational, randomized phase iii trial of iseganan hcl oral solution for reducing the severity of oral mucositis in patients receiving radiotherapy for head-andneck malignancy. Int. J. Radiat. Oncol. Biol. Phys. 2004, 58, 674-681.
    • (2004) Int. J. Radiat. Oncol. Biol. Phys. , vol.58 , pp. 674-681
    • Trotti, A.1    Garden, A.2    Warde, P.3    Symonds, P.4    Langer, C.5    Redman, R.6    Pajak, T.F.7    Fleming, T.R.8    Henke, M.9    Bourhis, J.10
  • 186
    • 79960961765 scopus 로고    scopus 로고
    • Proline-rich antimicrobial peptides: Converging to a non-lytic mechanism of action
    • Scocchi, M.; Tossi, A.; Gennaro, R. Proline-rich antimicrobial peptides: Converging to a non-lytic mechanism of action. Cell. Mol. Life Sci. 2011, 68, 2317-2330.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2317-2330
    • Scocchi, M.1    Tossi, A.2    Gennaro, R.3
  • 188
    • 0027216093 scopus 로고
    • Mechanisms of action on escherichia coli of cecropin p1 and pr-39, two antibacterial peptides from pig intestine
    • Boman, H.G.; Agerberth, B.; Boman, A. Mechanisms of action on escherichia coli of cecropin p1 and pr-39, two antibacterial peptides from pig intestine. Infect. Immun. 1993, 61, 2978-2984.
    • (1993) Infect. Immun. , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 190
    • 61649088165 scopus 로고    scopus 로고
    • Targeted engineering of the antibacterial peptide apidaecin, based on an in vivo monitoring assay system
    • Taguchi, S.; Mita, K.; Ichinohe, K.; Hashimoto, S. Targeted engineering of the antibacterial peptide apidaecin, based on an in vivo monitoring assay system. Appl. Environ. Microbiol. 2009, 75, 1460-1464.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 1460-1464
    • Taguchi, S.1    Mita, K.2    Ichinohe, K.3    Hashimoto, S.4
  • 191
    • 0024454751 scopus 로고
    • Apidaecins: Antibacterial peptides from honeybees
    • Casteels, P.; Ampe, C.; Jacobs, F.; Vaeck, M.; Tempst, P. Apidaecins: Antibacterial peptides from honeybees. EMBO J. 1989, 8, 2387-2391.
    • (1989) EMBO J. , vol.8 , pp. 2387-2391
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Vaeck, M.4    Tempst, P.5
  • 192
    • 0029929079 scopus 로고    scopus 로고
    • Enlarged scale chemical synthesis and range of activity of drosocin, an o-glycosylated antibacterial peptide of drosophila
    • Bulet, P.; Urge, L.; Ohresser, S.; Hetru, C.; Otvos, L., Jr. Enlarged scale chemical synthesis and range of activity of drosocin, an o-glycosylated antibacterial peptide of drosophila. Eur. J. Biochem. 1996, 238, 64-69.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 64-69
    • Bulet, P.1    Urge, L.2    Ohresser, S.3    Hetru, C.4    Otvos, L.5
  • 194
    • 0028304808 scopus 로고
    • Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug pyrrhocoris apterus
    • Cociancich, S.; Dupont, A.; Hegy, G.; Lanot, R.; Holder, F.; Hetru, C.; Hoffmann, J.A.; Bulet, P. Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug pyrrhocoris apterus. Biochem. J. 1994, 300(Pt 2), 567-575.
    • (1994) Biochem. J. , vol.300 , pp. 567-575
    • Cociancich, S.1    Dupont, A.2    Hegy, G.3    Lanot, R.4    Holder, F.5    Hetru, C.6    Hoffmann, J.A.7    Bulet, P.8
  • 197
    • 0028286667 scopus 로고
    • Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity
    • Casteels, P.; Tempst, P. Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity. Biochem. Biophys. Res. Commun. 1994, 199, 339-345.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 339-345
    • Casteels, P.1    Tempst, P.2
  • 198
    • 3142774800 scopus 로고    scopus 로고
    • Potential peptide carriers: Amphipathic proline-rich peptides derived from the n-terminal domain of gamma-zein
    • Fernandez-Carneado, J.; Kogan, M.J.; Castel, S.; Giralt, E. Potential peptide carriers: Amphipathic proline-rich peptides derived from the n-terminal domain of gamma-zein. Angew. Chem. Int. Ed. Engl. 2004, 43, 1811-1814.
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 1811-1814
    • Fernandez-Carneado, J.1    Kogan, M.J.2    Castel, S.3    Giralt, E.4
  • 199
    • 54049153545 scopus 로고    scopus 로고
    • Scope and limitations of the designer proline-rich antibacterial peptide dimer, a3-apo, alone or in synergy with conventional antibiotics
    • Cassone, M.; Vogiatzi, P.; La Montagna, R.; De Olivier Inacio, V.; Cudic, P.; Wade, J.D.; Otvos, L., Jr. Scope and limitations of the designer proline-rich antibacterial peptide dimer, a3-apo, alone or in synergy with conventional antibiotics. Peptides 2008, 29, 1878-1886.
    • (2008) Peptides , vol.29 , pp. 1878-1886
    • Cassone, M.1    Vogiatzi, P.2    La Montagna, R.3    De Olivier Inacio, V.4    Cudic, P.5    Wade, J.D.6    Otvos, L.7
  • 200
    • 36549087177 scopus 로고    scopus 로고
    • Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the spider crab, hyas araneus
    • Stensvag, K.; Haug, T.; Sperstad, S.V.; Rekdal, O.; Indrevoll, B.; Styrvold, O.B. Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the spider crab, hyas araneus. Dev. Comp. Immunol. 2008, 32, 275-285.
    • (2008) Dev. Comp. Immunol. , vol.32 , pp. 275-285
    • Stensvag, K.1    Haug, T.2    Sperstad, S.V.3    Rekdal, O.4    Indrevoll, B.5    Styrvold, O.B.6
  • 201
    • 84872237583 scopus 로고    scopus 로고
    • Structure-activity relationships of the antimicrobial peptide arasin 1 - And mode of action studies of the n-terminal, proline-rich region
    • Paulsen, V.S.; Blencke, H.M.; Benincasa, M.; Haug, T.; Eksteen, J.J.; Styrvold, O.B.; Scocchi, M.; Stensvag, K. Structure-activity relationships of the antimicrobial peptide arasin 1 - and mode of action studies of the n-terminal, proline-rich region. PloS ONE 2013, 8, e53326.
    • (2013) PloS ONE , vol.8
    • Paulsen, V.S.1    Blencke, H.M.2    Benincasa, M.3    Haug, T.4    Eksteen, J.J.5    Styrvold, O.B.6    Scocchi, M.7    Stensvag, K.8
  • 202
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial peptide pyrrhocoricin inhibits the atpase actions of dnak and prevents chaperone-assisted protein folding
    • Kragol, G.; Lovas, S.; Varadi, G.; Condie, B.A.; Hoffmann, R.; Otvos, L., Jr. The antibacterial peptide pyrrhocoricin inhibits the atpase actions of dnak and prevents chaperone-assisted protein folding. Biochemistry 2001, 40, 3016-3026.
    • (2001) Biochemistry , vol.40 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3    Condie, B.A.4    Hoffmann, R.5    Otvos, L.6
  • 205
    • 77955665054 scopus 로고    scopus 로고
    • Characterization of an abaecin-like antimicrobial peptide identified from a pteromalus puparum cdna clone
    • Shen, X.; Ye, G.; Cheng, X.; Yu, C.; Altosaar, I.; Hu, C. Characterization of an abaecin-like antimicrobial peptide identified from a pteromalus puparum cdna clone. J. Invertebr. Pathol. 2010, 105, 24-29.
    • (2010) J. Invertebr. Pathol. , vol.105 , pp. 24-29
    • Shen, X.1    Ye, G.2    Cheng, X.3    Yu, C.4    Altosaar, I.5    Hu, C.6
  • 206
    • 0035544532 scopus 로고    scopus 로고
    • Differential infectivity of two pseudomonas species and the immune response in the milkweed bug, oncopeltus fasciatus (insecta: Hemiptera)
    • Schneider, M.; Dorn, A. Differential infectivity of two pseudomonas species and the immune response in the milkweed bug, oncopeltus fasciatus (insecta: Hemiptera). J. Invertebr. Pathol. 2001, 78, 135-140.
    • (2001) J. Invertebr. Pathol. , vol.78 , pp. 135-140
    • Schneider, M.1    Dorn, A.2
  • 207
    • 84866444887 scopus 로고    scopus 로고
    • Absence of in vitro innate immunomodulation by insect-derived short proline-rich antimicrobial peptides points to direct antibacterial action in vivo
    • Fritsche, S.; Knappe, D.; Berthold, N.; von Buttlar, H.; Hoffmann, R.; Alber, G. Absence of in vitro innate immunomodulation by insect-derived short proline-rich antimicrobial peptides points to direct antibacterial action in vivo. J. Pept. Sci. 2012, 18, 599-608.
    • (2012) J. Pept. Sci. , vol.18 , pp. 599-608
    • Fritsche, S.1    Knappe, D.2    Berthold, N.3    von Buttlar, H.4    Hoffmann, R.5    Alber, G.6
  • 208
    • 84911468505 scopus 로고    scopus 로고
    • Insect-derived prolinerich antimicrobial peptides kill bacteria by inhibiting bacterial protein translation at the 70 s ribosome
    • Krizsan, A.; Volke, D.; Weinert, S.; Strater, N.; Knappe, D.; Hoffmann, R. Insect-derived prolinerich antimicrobial peptides kill bacteria by inhibiting bacterial protein translation at the 70 s ribosome. Angew. Chem. Int. Ed. Engl. 2014, 53, 12236-12239.
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , pp. 12236-12239
    • Krizsan, A.1    Volke, D.2    Weinert, S.3    Strater, N.4    Knappe, D.5    Hoffmann, R.6
  • 209
    • 84871591508 scopus 로고    scopus 로고
    • The lipid dependence of antimicrobial peptide activity is an unreliable experimental test for different pore models
    • Bobone, S.; Roversi, D.; Giordano, L.; De Zotti, M.; Formaggio, F.; Toniolo, C.; Park, Y.; Stella, L. The lipid dependence of antimicrobial peptide activity is an unreliable experimental test for different pore models. Biochemistry 2012, 51, 10124-10126.
    • (2012) Biochemistry , vol.51 , pp. 10124-10126
    • Bobone, S.1    Roversi, D.2    Giordano, L.3    De Zotti, M.4    Formaggio, F.5    Toniolo, C.6    Park, Y.7    Stella, L.8
  • 210
    • 84912532312 scopus 로고    scopus 로고
    • How many antimicrobial peptide molecules kill a bacterium? The case of pmap-23
    • Roversi, D.; Luca, V.; Aureli, S.; Park, Y.; Mangoni, M.L.; Stella, L. How many antimicrobial peptide molecules kill a bacterium? The case of pmap-23. ACS Chem. Biol. 2014, 9, 2003-2007.
    • (2014) ACS Chem. Biol. , vol.9 , pp. 2003-2007
    • Roversi, D.1    Luca, V.2    Aureli, S.3    Park, Y.4    Mangoni, M.L.5    Stella, L.6
  • 211
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H.W. Action of antimicrobial peptides: Two-state model. Biochemistry 2000, 39, 8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 212
    • 40949131305 scopus 로고    scopus 로고
    • Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes
    • Andrushchenko, V.V.; Aarabi, M.H.; Nguyen, L.T.; Prenner, E.J.; Vogel, H.J. Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes. Biochim. Biophys. Acta 2008, 1778, 1004-1014.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1004-1014
    • Andrushchenko, V.V.1    Aarabi, M.H.2    Nguyen, L.T.3    Prenner, E.J.4    Vogel, H.J.5
  • 213
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 214
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes
    • Kagan, B.L.; Selsted, M.E.; Ganz, T.; Lehrer, R.I. Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes. Proc. Natl. Acad. Sci. USA 1990, 87, 210-214.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4
  • 215
    • 15444370838 scopus 로고    scopus 로고
    • A molecular mechanism for lipopolysaccharide protection of gram-negative bacteria from antimicrobial peptides
    • Papo, N.; Shai, Y. A molecular mechanism for lipopolysaccharide protection of gram-negative bacteria from antimicrobial peptides. J. Biol. Chem. 2005, 280, 10378-10387.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10378-10387
    • Papo, N.1    Shai, Y.2
  • 216
    • 34548150567 scopus 로고    scopus 로고
    • Mechanisms of endotoxin neutralization by synthetic cationic compounds
    • Andra, J.; Gutsmann, T.; Garidel, P.; Brandenburg, K. Mechanisms of endotoxin neutralization by synthetic cationic compounds. J. Endotoxin Res. 2006, 12, 261-277.
    • (2006) J. Endotoxin Res. , vol.12 , pp. 261-277
    • Andra, J.1    Gutsmann, T.2    Garidel, P.3    Brandenburg, K.4
  • 218
    • 0033946014 scopus 로고    scopus 로고
    • Properties of cytotoxic peptide-formed ion channels
    • Kourie, J.I.; Shorthouse, A.A. Properties of cytotoxic peptide-formed ion channels. Am. J. Physiol. Cell. Physiol. 2000, 278, C1063-C1087.
    • (2000) Am. J. Physiol. Cell. Physiol. , vol.278 , pp. C1063-C1087
    • Kourie, J.I.1    Shorthouse, A.A.2
  • 220
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects
    • Steiner, H.; Andreu, D.; Merrifield, R.B. Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects. Biochim. Biophys. Acta 1988, 939, 260-266.
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 221
    • 0025738532 scopus 로고
    • Mechanism of mammalian cell lysis mediated by peptide defensins. Evidence for an initial alteration of the plasma membrane
    • Lichtenstein, A. Mechanism of mammalian cell lysis mediated by peptide defensins. Evidence for an initial alteration of the plasma membrane. J. Clin. Investig. 1991, 88, 93-100.
    • (1991) J. Clin. Investig. , vol.88 , pp. 93-100
    • Lichtenstein, A.1
  • 222
    • 0024391711 scopus 로고
    • Interaction of human defensins with escherichia coli. Mechanism of bactericidal activity
    • Lehrer, R.I.; Barton, A.; Daher, K.A.; Harwig, S.S.; Ganz, T.; Selsted, M.E. Interaction of human defensins with escherichia coli. Mechanism of bactericidal activity. J. Clin. Investig. 1989, 84, 553-561.
    • (1989) J. Clin. Investig. , vol.84 , pp. 553-561
    • Lehrer, R.I.1    Barton, A.2    Daher, K.A.3    Harwig, S.S.4    Ganz, T.5    Selsted, M.E.6
  • 223
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein, G.; Lecar, H. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys. 1977, 10, 1-34.
    • (1977) Q. Rev. Biophys. , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 224
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K.A. Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 2005, 3, 238-250.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 225
    • 84894255642 scopus 로고    scopus 로고
    • Antimicrobial peptide alamethicin insertion into lipid bilayer: A qcm-d exploration
    • Wang, K.F.; Nagarajan, R.; Camesano, T.A. Antimicrobial peptide alamethicin insertion into lipid bilayer: A qcm-d exploration. Colloid. Surface. B 2014, 116, 472-481.
    • (2014) Colloid. Surface. B , vol.116 , pp. 472-481
    • Wang, K.F.1    Nagarajan, R.2    Camesano, T.A.3
  • 226
    • 0028010959 scopus 로고
    • The barrel-stave model as applied to alamethicin and its analogs reevaluated
    • Laver, D.R. The barrel-stave model as applied to alamethicin and its analogs reevaluated. Biophys. J. 1994, 66, 355-359.
    • (1994) Biophys. J. , vol.66 , pp. 355-359
    • Laver, D.R.1
  • 228
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang, L.; Harroun, T.A.; Weiss, T.M.; Ding, L.; Huang, H.W. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 2001, 81, 1475-1485.
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 229
    • 52049109183 scopus 로고    scopus 로고
    • Toroidal pores formed by antimicrobial peptides show significant disorder
    • Sengupta, D.; Leontiadou, H.; Mark, A.E.; Marrink, S.J. Toroidal pores formed by antimicrobial peptides show significant disorder. Biochim. Biophys. Acta 2008, 1778, 2308-2317.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2308-2317
    • Sengupta, D.1    Leontiadou, H.2    Mark, A.E.3    Marrink, S.J.4
  • 230
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger, B.; Lohner, K. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta Biomembr. 2006, 1758, 1529-1539.
    • (2006) Biochim. Biophys. Acta Biomembr. , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 231
    • 68749115077 scopus 로고    scopus 로고
    • Rationalizing the membrane interactions of cationic amphipathic antimicrobial peptides by their molecular shape
    • Bechinger, B. Rationalizing the membrane interactions of cationic amphipathic antimicrobial peptides by their molecular shape. Curr. Opin. Colloid IN 2009, 14, 349-355.
    • (2009) Curr. Opin. Colloid IN , vol.14 , pp. 349-355
    • Bechinger, B.1
  • 233
    • 0036712127 scopus 로고    scopus 로고
    • Mechanism and kinetics of delta-lysin interaction with phospholipid vesicles
    • Pokorny, A.; Birkbeck, T.H.; Almeida, P.F.F. Mechanism and kinetics of delta-lysin interaction with phospholipid vesicles. Biochemistry 2002, 41, 11044-11056.
    • (2002) Biochemistry , vol.41 , pp. 11044-11056
    • Pokorny, A.1    Birkbeck, T.H.2    Almeida, P.F.F.3
  • 234
    • 33748942106 scopus 로고    scopus 로고
    • Interaction of the antimicrobial peptide pheromone plantaricin a with model membranes: Implications for a novel mechanism of action
    • Zhao, H.; Sood, R.; Jutila, A.; Bose, S.; Fimland, G.; Nissen-Meyer, J.; Kinnunen, P.K.J. Interaction of the antimicrobial peptide pheromone plantaricin a with model membranes: Implications for a novel mechanism of action. Biochim. Biophys. Acta Biomembr. 2006, 1758, 1461-1474.
    • (2006) Biochim. Biophys. Acta Biomembr. , vol.1758 , pp. 1461-1474
    • Zhao, H.1    Sood, R.2    Jutila, A.3    Bose, S.4    Fimland, G.5    Nissen-Meyer, J.6    Kinnunen, P.K.J.7
  • 235
    • 79953790729 scopus 로고    scopus 로고
    • Bacterial membrane lipids in the action of antimicrobial agents
    • Epand, R.M.; Epand, R.F. Bacterial membrane lipids in the action of antimicrobial agents. J. Pept. Sci. 2011, 17, 298-305.
    • (2011) J. Pept. Sci. , vol.17 , pp. 298-305
    • Epand, R.M.1    Epand, R.F.2
  • 236
    • 38349116218 scopus 로고    scopus 로고
    • Analysis of in vitro activities and modes of action of synthetic antimicrobial peptides derived from an alpha-helical 'sequence template'
    • Pag, U.; Oedenkoven, M.; Sass, V.; Shai, Y.; Shamova, O.; Antcheva, N.; Tossi, A.; Sahl, H.G. Analysis of in vitro activities and modes of action of synthetic antimicrobial peptides derived from an alpha-helical 'sequence template'. J. Antimicrob. Chemother. 2008, 61, 341-352.
    • (2008) J. Antimicrob. Chemother. , vol.61 , pp. 341-352
    • Pag, U.1    Oedenkoven, M.2    Sass, V.3    Shai, Y.4    Shamova, O.5    Antcheva, N.6    Tossi, A.7    Sahl, H.G.8
  • 238
    • 50049096434 scopus 로고    scopus 로고
    • Mode of action of human beta-defensin 3 against staphylococcus aureus and transcriptional analysis of responses to defensin challenge
    • Sass, V.; Pag, U.; Tossi, A.; Bierbaum, G.; Sahl, H.G. Mode of action of human beta-defensin 3 against staphylococcus aureus and transcriptional analysis of responses to defensin challenge. Int. J. Med. Microbiol. 2008, 298, 619-633.
    • (2008) Int. J. Med. Microbiol. , vol.298 , pp. 619-633
    • Sass, V.1    Pag, U.2    Tossi, A.3    Bierbaum, G.4    Sahl, H.G.5
  • 241
    • 0030068934 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from bufo bufo gargarizans
    • Park, C.B.; Kim, M.S.; Kim, S.C. A novel antimicrobial peptide from bufo bufo gargarizans. Biochem. Biophys. Res. Commun. 1996, 218, 408-413.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 408-413
    • Park, C.B.1    Kim, M.S.2    Kim, S.C.3
  • 242
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin ii: Buforin ii kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park, C.B.; Kim, H.S.; Kim, S.C. Mechanism of action of the antimicrobial peptide buforin ii: Buforin ii kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 1998, 244, 253-257.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 243
    • 33746910238 scopus 로고    scopus 로고
    • Apidaecin-type peptides: Biodiversity, structure-function relationships and mode of action
    • Li, W.F.; Ma, G.X.; Zhou, X.X. Apidaecin-type peptides: Biodiversity, structure-function relationships and mode of action. Peptides 2006, 27, 2350-2359.
    • (2006) Peptides , vol.27 , pp. 2350-2359
    • Li, W.F.1    Ma, G.X.2    Zhou, X.X.3
  • 244
    • 84859444332 scopus 로고    scopus 로고
    • Resistance to antimicrobial peptides in gram-negative bacteria
    • Gruenheid, S.; Le Moual, H. Resistance to antimicrobial peptides in gram-negative bacteria. FEMS Microbiol. Lett. 2012, 330, 81-89.
    • (2012) FEMS Microbiol. Lett. , vol.330 , pp. 81-89
    • Gruenheid, S.1    Le Moual, H.2
  • 245
    • 4544254599 scopus 로고    scopus 로고
    • Proteus mirabilis zapa metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides
    • Belas, R.; Manos, J.; Suvanasuthi, R. Proteus mirabilis zapa metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides. Infect. Immun. 2004, 72, 5159-5167.
    • (2004) Infect. Immun. , vol.72 , pp. 5159-5167
    • Belas, R.1    Manos, J.2    Suvanasuthi, R.3
  • 246
    • 34548067653 scopus 로고    scopus 로고
    • Omptin proteins: An expanding family of outer membrane proteases in gram-negative enterobacteriaceae
    • Hritonenko, V.; Stathopoulos, C. Omptin proteins: An expanding family of outer membrane proteases in gram-negative enterobacteriaceae. Mol. Membr. Biol. 2007, 24, 395-406.
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 395-406
    • Hritonenko, V.1    Stathopoulos, C.2
  • 247
  • 248
    • 66549099729 scopus 로고    scopus 로고
    • O-antigen-negative salmonella enterica serovar typhimurium is attenuated in intestinal colonization but elicits colitis in streptomycin-treated mice
    • Ilg, K.; Endt, K.; Misselwitz, B.; Stecher, B.; Aebi, M.; Hardt, W.D. O-antigen-negative salmonella enterica serovar typhimurium is attenuated in intestinal colonization but elicits colitis in streptomycin-treated mice. Infect. Immun. 2009, 77, 2568-2575.
    • (2009) Infect. Immun. , vol.77 , pp. 2568-2575
    • Ilg, K.1    Endt, K.2    Misselwitz, B.3    Stecher, B.4    Aebi, M.5    Hardt, W.D.6
  • 249
    • 65949101251 scopus 로고    scopus 로고
    • Inhibition of cathelicidin activity by bacterial exopolysaccharides
    • Foschiatti, M.; Cescutti, P.; Tossi, A.; Rizzo, R. Inhibition of cathelicidin activity by bacterial exopolysaccharides. Mol. Microbiol. 2009, 72, 1137-1146.
    • (2009) Mol. Microbiol. , vol.72 , pp. 1137-1146
    • Foschiatti, M.1    Cescutti, P.2    Tossi, A.3    Rizzo, R.4
  • 250
    • 58949097012 scopus 로고    scopus 로고
    • Capsule polysaccharide is a bacterial decoy for antimicrobial peptides
    • Llobet, E.; Tomas, J.M.; Bengoechea, J.A. Capsule polysaccharide is a bacterial decoy for antimicrobial peptides. Microbiology. 2008, 154, 3877-3886.
    • (2008) Microbiology. , vol.154 , pp. 3877-3886
    • Llobet, E.1    Tomas, J.M.2    Bengoechea, J.A.3
  • 252
    • 44649203366 scopus 로고    scopus 로고
    • The salmonella pmrab regulon: Lipopolysaccharide modifications, antimicrobial peptide resistance and more
    • Gunn, J.S. The salmonella pmrab regulon: Lipopolysaccharide modifications, antimicrobial peptide resistance and more. Trends Microbiol. 2008, 16, 284-290.
    • (2008) Trends Microbiol. , vol.16 , pp. 284-290
    • Gunn, J.S.1
  • 254
    • 84883539803 scopus 로고    scopus 로고
    • Adaptive evolution of escherichia coli to an alpha-peptide/beta-peptoid peptidomimetic induces stable resistance
    • Hein-Kristensen, L.; Franzyk, H.; Holch, A.; Gram, L. Adaptive evolution of escherichia coli to an alpha-peptide/beta-peptoid peptidomimetic induces stable resistance. PloS ONE 2013, 8, e73620.
    • (2013) PloS ONE , vol.8
    • Hein-Kristensen, L.1    Franzyk, H.2    Holch, A.3    Gram, L.4
  • 255
    • 0001066226 scopus 로고    scopus 로고
    • How intracellular bacteria survive: Surface modifications that promote resistance to host innate immune responses
    • Ernst, R.K.; Guina, T.; Miller, S.I. How intracellular bacteria survive: Surface modifications that promote resistance to host innate immune responses. J. Infect. Dis. 1999, 179, S326-S330.
    • (1999) J. Infect. Dis. , vol.179 , pp. S326-S330
    • Ernst, R.K.1    Guina, T.2    Miller, S.I.3
  • 256
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid a modifications by salmonella typhimurium virulence genes phop-phoq
    • Guo, L.; Lim, K.B.; Gunn, J.S.; Bainbridge, B.; Darveau, R.P.; Hackett, M.; Miller, S.I. Regulation of lipid a modifications by salmonella typhimurium virulence genes phop-phoq. Science 1997, 276, 250-253.
    • (1997) Science , vol.276 , pp. 250-253
    • Guo, L.1    Lim, K.B.2    Gunn, J.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6    Miller, S.I.7
  • 257
    • 0032538292 scopus 로고    scopus 로고
    • Lipid a acylation and bacterial resistance against vertebrate antimicrobial peptides
    • Guo, L.; Lim, K.B.; Poduje, C.M.; Daniel, M.; Gunn, J.S.; Hackett, M.; Miller, S.I. Lipid a acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell 1998, 95, 189-198.
    • (1998) Cell , vol.95 , pp. 189-198
    • Guo, L.1    Lim, K.B.2    Poduje, C.M.3    Daniel, M.4    Gunn, J.S.5    Hackett, M.6    Miller, S.I.7
  • 258
    • 85019669882 scopus 로고    scopus 로고
    • Antimicrobial peptide resistance mechanisms of gram-positive bacteria
    • Nawrocki, K.L.; Crispell, E.K.; McBride, S.M. Antimicrobial peptide resistance mechanisms of gram-positive bacteria. Antibiotics (Basel) 2014, 3, 461-492.
    • (2014) Antibiotics (Basel) , vol.3 , pp. 461-492
    • Nawrocki, K.L.1    Crispell, E.K.2    McBride, S.M.3
  • 259
    • 84937640687 scopus 로고    scopus 로고
    • Identification of anti-biofilm components in withania somnifera and their effect on virulence of streptococcus mutans biofilms
    • Pandit, S.; Cai, J.N.; Song, K.Y.; Jeon, J.G. Identification of anti-biofilm components in withania somnifera and their effect on virulence of streptococcus mutans biofilms. J. Appl. Microbiol. 2015, doi:10.1111/jam.12851.
    • (2015) J. Appl. Microbiol.
    • Pandit, S.1    Cai, J.N.2    Song, K.Y.3    Jeon, J.G.4
  • 260
    • 84929667079 scopus 로고    scopus 로고
    • Measurements in pediatric patients with cardiomyopathies: Comparison of cardiac magnetic resonance imaging and echocardiography
    • Zhang, Y.; He, L.; Cai, J.; Lv, T.; Yi, Q.; Xu, Y.; Liu, L.; Zhu, J.; Tian, J. Measurements in pediatric patients with cardiomyopathies: Comparison of cardiac magnetic resonance imaging and echocardiography. Cardiology 2015, 131, 245-250.
    • (2015) Cardiology , vol.131 , pp. 245-250
    • Zhang, Y.1    He, L.2    Cai, J.3    Lv, T.4    Yi, Q.5    Xu, Y.6    Liu, L.7    Zhu, J.8    Tian, J.9
  • 261
    • 84937891732 scopus 로고    scopus 로고
    • Cw dual-frequency mopa laser with frequency separation of 45 ghz
    • Hu, M.; Zheng, Y.; Cai, J.; Zhang, G.; Li, Q.; Zhou, X.; Wei, Y.; Lu, Y. Cw dual-frequency mopa laser with frequency separation of 45 ghz. Opt. Express 2015, 23, 9881-9889.
    • (2015) Opt. Express , vol.23 , pp. 9881-9889
    • Hu, M.1    Zheng, Y.2    Cai, J.3    Zhang, G.4    Li, Q.5    Zhou, X.6    Wei, Y.7    Lu, Y.8
  • 262
    • 84927552904 scopus 로고    scopus 로고
    • 293ft is a highly suitable mammalian cell line for the in vitro enzymatic activity analysis of typical p450 proteins
    • Dai, D.P.; Geng, P.W.; Cai, J.; Wang, S.H.; Nic, J.J.; Hu, J.H.; Hu, G.X.; Cai, J.P. 293ft is a highly suitable mammalian cell line for the in vitro enzymatic activity analysis of typical p450 proteins. Pharmazie 2015, 70, 33-37.
    • (2015) Pharmazie , vol.70 , pp. 33-37
    • Dai, D.P.1    Geng, P.W.2    Cai, J.3    Wang, S.H.4    Nic, J.J.5    Hu, J.H.6    Hu, G.X.7    Cai, J.P.8
  • 263
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a, member of the resistance/nodulation/division efflux pump family
    • Shafer, W.M.; Qu, X.D.; Waring, A.J.; Lehrer, R.I. Modulation of neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a, member of the resistance/nodulation/division efflux pump family. Proc. Natl. Acad. Sci. USA 1998, 95, 1829- 1833.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.D.2    Waring, A.J.3    Lehrer, R.I.4
  • 264
    • 0027445662 scopus 로고
    • Molecular-genetic analysis of a locus required for resistance to antimicrobial peptides in salmonella-typhimurium
    • Parralopez, C.; Baer, M.T.; Groisman, E.A. Molecular-genetic analysis of a locus required for resistance to antimicrobial peptides in salmonella-typhimurium. EMBO J. 1993, 12, 4053-4062.
    • (1993) EMBO J. , vol.12 , pp. 4053-4062
    • Parralopez, C.1    Baer, M.T.2    Groisman, E.A.3
  • 266
    • 0015603328 scopus 로고
    • A new antibiotic, leucinostatin, derived from penicillium lilacinum
    • Arai, T.; Mikami, Y.; Fukushima, K.; Utsumi, T.; Yazawa, K. A new antibiotic, leucinostatin, derived from penicillium lilacinum. J. Antibiot. 1973, 26, 157-161.
    • (1973) J. Antibiot. , vol.26 , pp. 157-161
    • Arai, T.1    Mikami, Y.2    Fukushima, K.3    Utsumi, T.4    Yazawa, K.5
  • 267
    • 79959936150 scopus 로고    scopus 로고
    • Investigating the cationic side chains of the antimicrobial peptide tritrpticin: Hydrogen bonding properties govern its membrane-disruptive activities
    • Nguyen, L.T.; de Boer, L.; Zaat, S.A.; Vogel, H.J. Investigating the cationic side chains of the antimicrobial peptide tritrpticin: Hydrogen bonding properties govern its membrane-disruptive activities. Biochim. Biophys. Acta 2011, 1808, 2297-2303.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2297-2303
    • Nguyen, L.T.1    de Boer, L.2    Zaat, S.A.3    Vogel, H.J.4
  • 268
    • 70350173842 scopus 로고    scopus 로고
    • Peptidomimetics - A versatile route to biologically active compounds
    • Grauer, A.; Konig, B. Peptidomimetics - a versatile route to biologically active compounds. Eur. J. Org. Chem. 2009, 5099-5111.
    • (2009) Eur. J. Org. Chem. , pp. 5099-5111
    • Grauer, A.1    Konig, B.2
  • 269
    • 0025001650 scopus 로고
    • All-d-magainin: Chirality, antimicrobial activity and proteolytic resistance
    • Bessalle, R.; Kapitkovsky, A.; Gorea, A.; Shalit, I.; Fridkin, M. All-d-magainin: Chirality, antimicrobial activity and proteolytic resistance. FEBS Lett. 1990, 274, 151-155.
    • (1990) FEBS Lett. , vol.274 , pp. 151-155
    • Bessalle, R.1    Kapitkovsky, A.2    Gorea, A.3    Shalit, I.4    Fridkin, M.5
  • 270
    • 79960950287 scopus 로고    scopus 로고
    • Beyond natural antimicrobial peptides: Multimeric peptides and other peptidomimetic approaches
    • Giuliani, A.; Rinaldi, A.C. Beyond natural antimicrobial peptides: Multimeric peptides and other peptidomimetic approaches. Cell. Mol. Life Sci. 2011, 68, 2255-2266.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2255-2266
    • Giuliani, A.1    Rinaldi, A.C.2
  • 271
    • 33646937528 scopus 로고    scopus 로고
    • Consequences of n-acylation on structure and membrane binding properties of dermaseptin derivative k4-s4-(1-13)
    • Shalev, D.E.; Rotem, S.; Fish, A.; Mor, A. Consequences of n-acylation on structure and membrane binding properties of dermaseptin derivative k4-s4-(1-13). J. Biol. Chem. 2006, 281, 9432-9438.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9432-9438
    • Shalev, D.E.1    Rotem, S.2    Fish, A.3    Mor, A.4
  • 273
    • 84896326517 scopus 로고    scopus 로고
    • In vitro and in vivo activities of novel cyclic lipopeptides against staphylococcal biofilms
    • Bionda, N.; Pastar, I.; Davis, S.C.; Cudic, P. In vitro and in vivo activities of novel cyclic lipopeptides against staphylococcal biofilms. Protein pept. Lett. 2014, 21, 352-356.
    • (2014) Protein pept. Lett. , vol.21 , pp. 352-356
    • Bionda, N.1    Pastar, I.2    Davis, S.C.3    Cudic, P.4
  • 275
    • 77249095412 scopus 로고    scopus 로고
    • Antimicrobial activity of small beta-peptidomimetics based on the pharmacophore model of short cationic antimicrobial peptides
    • Hansen, T.; Alst, T.; Havelkova, M.; Strom, M.B. Antimicrobial activity of small beta-peptidomimetics based on the pharmacophore model of short cationic antimicrobial peptides. J. Med. Chem. 2010, 53, 595-606.
    • (2010) J. Med. Chem. , vol.53 , pp. 595-606
    • Hansen, T.1    Alst, T.2    Havelkova, M.3    Strom, M.B.4
  • 276
    • 84931957325 scopus 로고    scopus 로고
    • Molecular and cytological comparisons of chromosomes 7el, 7el, 7e, and 7e derived from thinopyrum
    • Guo, J.; He, F.; Cai, J.J.; Wang, H.W.; Li, A.F.; Wang, H.G.; Kong, L.R. Molecular and cytological comparisons of chromosomes 7el, 7el, 7e, and 7e derived from thinopyrum. Cytogenet. Genome Res. 2015, 145, 68-74.
    • (2015) Cytogenet. Genome Res. , vol.145 , pp. 68-74
    • Guo, J.1    He, F.2    Cai, J.J.3    Wang, H.W.4    Li, A.F.5    Wang, H.G.6    Kong, L.R.7
  • 277
    • 0034822676 scopus 로고    scopus 로고
    • Peptoid oligomers with alpha-chiral, aromatic side chains: Effects of chain length on secondary structure
    • Wu, C.W.; Sanborn, T.J.; Zuckermann, R.N.; Barron, A.E. Peptoid oligomers with alpha-chiral, aromatic side chains: Effects of chain length on secondary structure. J. Am. Chem. Soc. 2001, 123, 2958-2963.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2958-2963
    • Wu, C.W.1    Sanborn, T.J.2    Zuckermann, R.N.3    Barron, A.E.4
  • 278
    • 0034835809 scopus 로고    scopus 로고
    • Peptoid oligomers with alpha-chiral, aromatic side chains: Sequence requirements for the formation of stable peptoid helices
    • Wu, C.W.; Sanborn, T.J.; Huang, K.; Zuckermann, R.N.; Barron, A.E. Peptoid oligomers with alpha-chiral, aromatic side chains: Sequence requirements for the formation of stable peptoid helices. J. Am. Chem. Soc. 2001, 123, 6778-6784.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6778-6784
    • Wu, C.W.1    Sanborn, T.J.2    Huang, K.3    Zuckermann, R.N.4    Barron, A.E.5
  • 279
    • 0036143238 scopus 로고    scopus 로고
    • Extreme stability of helices formed by water-soluble poly-n-substituted glycines (polypeptoids) with alpha-chiral side chains
    • Sanborn, T.J.; Wu, C.W.; Zuckermann, R.N.; Barron, A.E. Extreme stability of helices formed by water-soluble poly-n-substituted glycines (polypeptoids) with alpha-chiral side chains. Biopolymers 2002, 63, 12-20.
    • (2002) Biopolymers , vol.63 , pp. 12-20
    • Sanborn, T.J.1    Wu, C.W.2    Zuckermann, R.N.3    Barron, A.E.4
  • 280
    • 44449096081 scopus 로고    scopus 로고
    • High-throughput evaluation of relative cell permeability between peptoids and peptides
    • Tan, N.C.; Yu, P.; Kwon, Y.U.; Kodadek, T. High-throughput evaluation of relative cell permeability between peptoids and peptides. Bioorg. Med. Chem. 2008, 16, 5853-5861.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 5853-5861
    • Tan, N.C.1    Yu, P.2    Kwon, Y.U.3    Kodadek, T.4
  • 281
    • 77957077791 scopus 로고    scopus 로고
    • A novel trp-rich model antimicrobial peptoid with increased protease stability
    • Bang, J.K.; Nan, Y.H.; Lee, E.K.; Shin, S.Y. A novel trp-rich model antimicrobial peptoid with increased protease stability. Bull. Korean Chem. Soc. 2010, 31, 2509-2513.
    • (2010) Bull. Korean Chem. Soc. , vol.31 , pp. 2509-2513
    • Bang, J.K.1    Nan, Y.H.2    Lee, E.K.3    Shin, S.Y.4
  • 283
    • 0141888597 scopus 로고    scopus 로고
    • Helical peptoid mimics of magainin-2 amide
    • Patch, J.A.; Barron, A.E. Helical peptoid mimics of magainin-2 amide. J. Am. Chem. Soc. 2003, 125, 12092-12093.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12092-12093
    • Patch, J.A.1    Barron, A.E.2
  • 286
    • 80054678276 scopus 로고    scopus 로고
    • Functional synergy between antimicrobial peptoids and peptides against gram-negative bacteria
    • Chongsiriwatana, N.P.; Wetzler, M.; Barron, A.E. Functional synergy between antimicrobial peptoids and peptides against gram-negative bacteria. Antimicrob. Agents Chemother. 2011, 55, 5399-5402.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 5399-5402
    • Chongsiriwatana, N.P.1    Wetzler, M.2    Barron, A.E.3
  • 287
    • 84935900157 scopus 로고    scopus 로고
    • Structure-activity relationship study of novel peptoids that mimic the structure of antimicrobial peptides
    • Mojsoska, B., Zuckermann, R.N., Jenssen, H. Structure-activity relationship study of novel peptoids that mimic the structure of antimicrobial peptides. Antimicrob. Agents Chemother. 2015, 59, 4112-4120.
    • (2015) Antimicrob. Agents Chemother. , vol.59 , pp. 4112-4120
    • Mojsoska, B.1    Zuckermann, R.N.2    Jenssen, H.3
  • 289
    • 84555188465 scopus 로고    scopus 로고
    • A comparison of linear and cyclic peptoid oligomers as potent antimicrobial agents
    • Huang, M.L.; Shin, S.B.; Benson, M.A.; Torres, V.J.; Kirshenbaum, K. A comparison of linear and cyclic peptoid oligomers as potent antimicrobial agents. ChemMedChem 2012, 7, 114-122.
    • (2012) ChemMedChem , vol.7 , pp. 114-122
    • Huang, M.L.1    Shin, S.B.2    Benson, M.A.3    Torres, V.J.4    Kirshenbaum, K.5
  • 290
    • 84878802687 scopus 로고    scopus 로고
    • Amphiphilic cyclic peptoids that exhibit antimicrobial activity by disrupting staphylococcus aureus membranes
    • Huang, M.L.; Benson, M.A.; Shin, S.B.Y.; Torres, V.J.; Kirshenbaum, K. Amphiphilic cyclic peptoids that exhibit antimicrobial activity by disrupting staphylococcus aureus membranes. Eur. J. Org. Chem. 2013, 3560-3566.
    • (2013) Eur. J. Org. Chem. , pp. 3560-3566
    • Huang, M.L.1    Benson, M.A.2    Shin, S.B.Y.3    Torres, V.J.4    Kirshenbaum, K.5
  • 291
    • 69049111808 scopus 로고    scopus 로고
    • Substitution of the arginine/leucine residues in apidaecin ib with peptoid residues: Effect on antimicrobial activity, cellular uptake, and proteolytic degradation
    • Gobbo, M.; Benincasa, M.; Bertoloni, G.; Biondi, B.; Dosselli, R.; Papini, E.; Reddi, E.; Rocchi, R.; Tavano, R.; Gennaro, R. Substitution of the arginine/leucine residues in apidaecin ib with peptoid residues: Effect on antimicrobial activity, cellular uptake, and proteolytic degradation. J. Med. Chem. 2009, 52, 5197-5206.
    • (2009) J. Med. Chem. , vol.52 , pp. 5197-5206
    • Gobbo, M.1    Benincasa, M.2    Bertoloni, G.3    Biondi, B.4    Dosselli, R.5    Papini, E.6    Reddi, E.7    Rocchi, R.8    Tavano, R.9    Gennaro, R.10
  • 292
    • 77955658045 scopus 로고    scopus 로고
    • Structural flexibility and the positive charges are the key factors in bacterial cell selectivity and membrane penetration of peptoid-substituted analog of piscidin 1
    • Kim, J.K.; Lee, S.A.; Shin, S.; Lee, J.Y.; Jeong, K.W.; Nan, Y.H.; Park, Y.S.; Shin, S.Y.; Kim, Y. Structural flexibility and the positive charges are the key factors in bacterial cell selectivity and membrane penetration of peptoid-substituted analog of piscidin 1. Biochim. Biophys. Acta Biomembr. 2010, 1798, 1913-1925.
    • (2010) Biochim. Biophys. Acta Biomembr. , vol.1798 , pp. 1913-1925
    • Kim, J.K.1    Lee, S.A.2    Shin, S.3    Lee, J.Y.4    Jeong, K.W.5    Nan, Y.H.6    Park, Y.S.7    Shin, S.Y.8    Kim, Y.9
  • 293
    • 84871669942 scopus 로고    scopus 로고
    • High in vitro antimicrobial activity of beta-peptoid-peptide hybrid oligomers against planktonic and biofilm cultures of staphylococcus epidermidis
    • Liu, Y.; Knapp, K.M.; Yang, L.; Molin, S.; Franzyk, H.; Folkesson, A. High in vitro antimicrobial activity of beta-peptoid-peptide hybrid oligomers against planktonic and biofilm cultures of staphylococcus epidermidis. Int. J. Antimicrob. Agents 2013, 41, 20-27.
    • (2013) Int. J. Antimicrob. Agents , vol.41 , pp. 20-27
    • Liu, Y.1    Knapp, K.M.2    Yang, L.3    Molin, S.4    Franzyk, H.5    Folkesson, A.6
  • 295
    • 77954373564 scopus 로고    scopus 로고
    • Antimicrobial, hemolytic, and cytotoxic activities of beta-peptoid-peptide hybrid oligomers: Improved properties compared to natural amps
    • Olsen, C.A.; Ziegler, H.L.; Nielsen, H.M.; Frimodt-Moller, N.; Jaroszewski, J.W.; Franzyk, H. Antimicrobial, hemolytic, and cytotoxic activities of beta-peptoid-peptide hybrid oligomers: Improved properties compared to natural amps. Chembiochem 2010, 11, 1356-1360.
    • (2010) Chembiochem , vol.11 , pp. 1356-1360
    • Olsen, C.A.1    Ziegler, H.L.2    Nielsen, H.M.3    Frimodt-Moller, N.4    Jaroszewski, J.W.5    Franzyk, H.6
  • 296
    • 49649115502 scopus 로고    scopus 로고
    • Dimeric building blocks for solid-phase synthesis of alpha-peptide-beta-peptoid chimeras
    • Bonke, G.; Vedel, L.; Witt, M.; Jaroszewski, J.W.; Olsen, C.A.; Franzyk, H. Dimeric building blocks for solid-phase synthesis of alpha-peptide-beta-peptoid chimeras. Synth. Stuttg. 2008, 2381-2390.
    • (2008) Synth. Stuttg. , pp. 2381-2390
    • Bonke, G.1    Vedel, L.2    Witt, M.3    Jaroszewski, J.W.4    Olsen, C.A.5    Franzyk, H.6
  • 297
    • 28044446984 scopus 로고    scopus 로고
    • Novel lysine-peptoid hybrids with antibacterial properties
    • Ryge, T.S.; Hansen, P.R. Novel lysine-peptoid hybrids with antibacterial properties. J. Pept. Sci. 2005, 11, 727-734.
    • (2005) J. Pept. Sci. , vol.11 , pp. 727-734
    • Ryge, T.S.1    Hansen, P.R.2
  • 298
    • 84886797920 scopus 로고    scopus 로고
    • Characterization of a proteolytically stable multifunctional host defense peptidomimetic
    • Jahnsen, R.D.; Haney, E.F.; Franzyk, H.; Hancock, R.E. Characterization of a proteolytically stable multifunctional host defense peptidomimetic. Chem. Biol. 2013, 20, 1286-1295.
    • (2013) Chem. Biol. , vol.20 , pp. 1286-1295
    • Jahnsen, R.D.1    Haney, E.F.2    Franzyk, H.3    Hancock, R.E.4
  • 300
    • 84937511431 scopus 로고    scopus 로고
    • Efficacy of oral etoposide in pretreated metastatic breast cancer: A multicenter phase 2 study
    • Yuan, P.; Di, L.; Zhang, X.; Yan, M.; Wan, D.; Li, L.; Zhang, Y.; Cai, J.; Dai, H.; Zhu, Q.; et al. Efficacy of oral etoposide in pretreated metastatic breast cancer: A multicenter phase 2 study. Medicine 2015, 94, e774.
    • (2015) Medicine , vol.94
    • Yuan, P.1    Di, L.2    Zhang, X.3    Yan, M.4    Wan, D.5    Li, L.6    Zhang, Y.7    Cai, J.8    Dai, H.9    Zhu, Q.10
  • 302
    • 84929877600 scopus 로고    scopus 로고
    • Protective effect of spironolactone on endothelial-to-mesenchymal transition in huvecs via notch pathway
    • Chen, X.; Cai, J.; Zhou, X.; Chen, L.; Gong, Y.; Gao, Z.; Zhang, H.; Huang, W.; Zhou, H. Protective effect of spironolactone on endothelial-to-mesenchymal transition in huvecs via notch pathway. Cell. Physiol. Biochem. 2015, 36, 191-200.
    • (2015) Cell. Physiol. Biochem. , vol.36 , pp. 191-200
    • Chen, X.1    Cai, J.2    Zhou, X.3    Chen, L.4    Gong, Y.5    Gao, Z.6    Zhang, H.7    Huang, W.8    Zhou, H.9
  • 303
    • 84930216318 scopus 로고    scopus 로고
    • Development of fluorescence sensing material based on cdse/zns quantum dots and molecularly imprinted polymer for the detection of carbaryl in rice and chinese cabbage
    • Zhang, C.; Cui, H.; Cai, J.; Duan, Y.; Liu, Y. Development of fluorescence sensing material based on cdse/zns quantum dots and molecularly imprinted polymer for the detection of carbaryl in rice and chinese cabbage. J. Agric. Food Chem. 2015, 63, 4966-4972.
    • (2015) J. Agric. Food Chem. , vol.63 , pp. 4966-4972
    • Zhang, C.1    Cui, H.2    Cai, J.3    Duan, Y.4    Liu, Y.5
  • 304
    • 12344320524 scopus 로고    scopus 로고
    • Application of 'inductive' qsar descriptors for quantification of antibacterial activity of cationic polypeptides
    • Cherkasov, A.; Jankovic, B. Application of 'inductive' qsar descriptors for quantification of antibacterial activity of cationic polypeptides. Molecules 2004, 9, 1034-1052.
    • (2004) Molecules , vol.9 , pp. 1034-1052
    • Cherkasov, A.1    Jankovic, B.2
  • 307
    • 79956000536 scopus 로고    scopus 로고
    • Knowledge-based computational methods for identifying or designing novel, non-homologous antimicrobial peptides
    • Juretic, D.; Vukicevic, D.; Petrov, D.; Novkovic, M.; Bojovic, V.; Lucic, B.; Ilic, N.; Tossi, A. Knowledge-based computational methods for identifying or designing novel, non-homologous antimicrobial peptides. Eur. Biophys. J. 2011, 40, 371-385.
    • (2011) Eur. Biophys. J. , vol.40 , pp. 371-385
    • Juretic, D.1    Vukicevic, D.2    Petrov, D.3    Novkovic, M.4    Bojovic, V.5    Lucic, B.6    Ilic, N.7    Tossi, A.8
  • 308
    • 84872106766 scopus 로고    scopus 로고
    • Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences
    • Ilic, N.; Novkovic, M.; Guida, F.; Xhindoli, D.; Benincasa, M.; Tossi, A.; Juretic, D. Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences. Biochim. Biophys. Acta 2013, 1828, 1004-1012.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1004-1012
    • Ilic, N.1    Novkovic, M.2    Guida, F.3    Xhindoli, D.4    Benincasa, M.5    Tossi, A.6    Juretic, D.7
  • 309
    • 60749130267 scopus 로고    scopus 로고
    • Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs
    • Cherkasov, A.; Hilpert, K.; Jenssen, H.; Fjell, C.D.; Waldbrook, M.; Mullaly, S.C.; Volkmer, R.; Hancock, R.E.W. Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs. ACS Chem. Biol. 2009, 4, 65-74.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 65-74
    • Cherkasov, A.1    Hilpert, K.2    Jenssen, H.3    Fjell, C.D.4    Waldbrook, M.5    Mullaly, S.C.6    Volkmer, R.7    Hancock, R.E.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.