메뉴 건너뛰기




Volumn 16, Issue 11, 2016, Pages 1217-1230

Short antimicrobial peptides and peptide scaffolds as promising antibacterial agents

Author keywords

Antibacterial peptidomimetics; Antibiotics; Antimicrobial peptides; Bacterial resistance; Cationic amphiphiles; Host defense peptides

Indexed keywords

4 AMINOPROLINE; ACYLDEPSIPEPTIDE; AMPHOPHILE; ARGININE; ARGININE RICH SHORT ANTIMICROBIAL PEPTIDE; BRILACIDIN; CECROPIN; DAPTOMYCIN; DEFENSIN; DIAMINOBUTYRIC ACID; EMPEDOPEPTIN; LACTOFERRIN 11 324; M 6; MAGAININ DERIVATIVE; MOLECULAR SCAFFOLD; MUREPAVADIN; OCTA 1; PEPTIDOMIMETIC AGENT; PLUSBACIN; POLYMYXIN DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; PROLINE; PROLINE RICH SHORT ANTIMICROBIAL PEPTIDE; RUTHENOCENE DERIVATIVE; STYLISIN; SUROTOMYCIN; TRIPROPEPTIN; TRYPTOPHAN; TRYPTOPHAN RICH SHORT ANTIMICROBIAL PEPTIDE; ULTRASHORT ANTIMICROBIAL PEPTIDE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; PEPTIDE;

EID: 84961721905     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026615666150915112459     Document Type: Article
Times cited : (43)

References (136)
  • 2
    • 84875262522 scopus 로고    scopus 로고
    • A call for antibiotic alternative research
    • Stanton, T.B. A call for antibiotic alternative research. Trends Microbiol., 2013, 21, 111-113.
    • (2013) Trends Microbiol. , vol.21 , pp. 111-113
    • Stanton, T.B.1
  • 3
    • 84901917759 scopus 로고    scopus 로고
    • An overview of antimicrobial resistance and its public health significance
    • Balsalobre, L.C.; Dropa, M.; Matté, M.H. An overview of antimicrobial resistance and its public health significance. Braz. J. Microbiol., 2014, 45, 1-5.
    • (2014) Braz. J. Microbiol. , vol.45 , pp. 1-5
    • Balsalobre, L.C.1    Dropa, M.2    Matté, M.H.3
  • 4
    • 84961756439 scopus 로고    scopus 로고
    • World Health Organization. Antimicrobial resistance: global report on surveillance
    • World Health Organization. Antimicrobial resistance: global report on surveillance. http://www.who.int/drugresistance/documents/surveillancereport/en/ (Accessed August 28, 2014).
  • 5
  • 6
    • 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
  • 8
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin – isolation, characterization of 2 active forms, and partial cDNA sequence of aprecursor
    • Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin – isolation, characterization of 2 active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. U.S.A., 1987, 84, 5449-5453.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 9
    • 34247117757 scopus 로고    scopus 로고
    • Cationic host defence peptides: Innate immune regulatory peptides as novel approach for treating infections
    • Mookherjee, N.; Hancock, R.E. Cationic host defence peptides: innate immune regulatory peptides as novel approach for treating infections. Cell. Mol. Life Sci., 2007, 64, 922-933.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 922-933
    • Mookherjee, N.1    Hancock, R.E.2
  • 10
    • 84872020895 scopus 로고    scopus 로고
    • Host defense peptides: An alternative as antiinfective and immunomodulatory therapeutics
    • Alba, A.; López-Abarrategui, C.; Otero-González, A.J. Host defense peptides: an alternative as antiinfective and immunomodulatory therapeutics. Biopolymers, 2012, 98, 251-267.
    • (2012) Biopolymers , vol.98 , pp. 251-267
    • Alba, A.1    López-Abarrategui, C.2    Otero-González, A.J.3
  • 11
    • 79960931688 scopus 로고    scopus 로고
    • Host-defense peptides: From biology to therapeutic strategies
    • Mangoni, M.L. Host-defense peptides: from biology to therapeutic strategies. Cell. Mol. Life Sci., 2011, 68, 2157-2159.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2157-2159
    • Mangoni, M.L.1
  • 12
    • 84887915050 scopus 로고    scopus 로고
    • Immune modulation by multifaceted cationic host defense (Antimicrobial) peptides
    • Hilchie, A.L.; Wuerth, K.; Hancock, R.E. Immune modulation by multifaceted cationic host defense (antimicrobial) peptides. Nat. Chem. Biol., 2013, 9, 761-768.
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 761-768
    • Hilchie, A.L.1    Wuerth, K.2    Hancock, R.E.3
  • 13
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense
    • Lai, Y.; Gallo, R.L. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol., 2009, 30, 131-141.
    • (2009) Trends Immunol. , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 14
    • 84871027267 scopus 로고    scopus 로고
    • Comprehensive summary of LL-37, the factotum human cathelicidin peptide
    • Vandamme, D.; Landuyt, B.; Luyten, W.; Schoofs, L. A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cell. Immunol., 2012, 280, 22-35.
    • (2012) Cell. Immunol. , vol.280 , pp. 22-35
    • Vandamme, D.1    Landuyt, B.2    Luyten, W.3    Schoofs, L.A.4
  • 15
    • 84868093334 scopus 로고    scopus 로고
    • Induction of the human cathelicidin LL-37 as a novel treatment against bacterial infections
    • van der Does, A.M.; Bergman, P.; Agerberth, B.; Lindbom, L. Induction of the human cathelicidin LL-37 as a novel treatment against bacterial infections. J. Leuokoc. Biol., 2012, 92, 735-742.
    • (2012) J. Leuokoc. Biol. , vol.92 , pp. 735-742
    • Van Der Does, A.M.1    Bergman, P.2    Agerberth, B.3    Lindbom, L.4
  • 19
    • 4444235598 scopus 로고    scopus 로고
    • Bacterial products increase expression of the human cathelicidin hCAP-18/LL-37 in cultured human sinus epithelial cells
    • Nell, M.J.; Tjabringa, G.S.; Vonk, M.J.; Hiemstra, P.S.; Grote, J.J. Bacterial products increase expression of the human cathelicidin hCAP-18/LL-37 in cultured human sinus epithelial cells. FEMS Immunol. Med. Microbiol., 2004, 42, 225-231.
    • (2004) FEMS Immunol. Med. Microbiol. , vol.42 , pp. 225-231
    • Nell, M.J.1    Tjabringa, G.S.2    Vonk, M.J.3    Hiemstra, P.S.4    Grote, J.J.5
  • 20
    • 36849009383 scopus 로고
    • Aerosporin, an antibiotic produced by Bacillus aerosporus Greer
    • Ainsworth, G.C.; Brown, A.M.; Brownlee, G. Aerosporin, an antibiotic produced by Bacillus aerosporus Greer. Nature, 1947, 159, 263.
    • (1947) Nature , vol.159 , pp. 263
    • Ainsworth, G.C.1    Brown, A.M.2    Brownlee, G.3
  • 24
    • 77949346087 scopus 로고    scopus 로고
    • Structure— activity relationships of polymyxin antibiotics
    • Velkov, T.; Thompson, P.E.; Nation, R.L.; Li, J. Structure— activity relationships of polymyxin antibiotics. J. Med. Chem., 2010, 53, 1898-1916.
    • (2010) J. Med. Chem. , vol.53 , pp. 1898-1916
    • Velkov, T.1    Thompson, P.E.2    Nation, R.L.3    Li, J.4
  • 25
    • 84878293341 scopus 로고    scopus 로고
    • Pharmacology of polymyxins: New insights into an ‘old’ class of antibiotics.
    • Velkov, T.; Roberts, K.D.; Nation, R.L.; Thompson, P.E.; Li, J. Pharmacology of polymyxins: new insights into an ‘old’ class of antibiotics., Future Microbiol., 2013, 8, 711-724.
    • (2013) Future Microbiol. , vol.8 , pp. 711-724
    • Velkov, T.1    Roberts, K.D.2    Nation, R.L.3    Thompson, P.E.4    Li, J.5
  • 26
    • 84896804072 scopus 로고    scopus 로고
    • A secondary mode of action of polymyxins against Gram-negative bacteria involves the inhibition of NADH-quinone oxidoreductase activity
    • Deris, Z.Z.; Akter, J.; Sivanesan, S.; Roberts, K.D.; Thompson, P.E.; Nation, R.L.; Li, J.; Velkov, T. A secondary mode of action of polymyxins against Gram-negative bacteria involves the inhibition of NADH-quinone oxidoreductase activity. J. Antibiot. (Tokyo), 2014, 67, 147-151.
    • (2014) J. Antibiot. (Tokyo) , vol.67 , pp. 147-151
    • Deris, Z.Z.1    Akter, J.2    Sivanesan, S.3    Roberts, K.D.4    Thompson, P.E.5    Nation, R.L.6    Li, J.7    Velkov, T.8
  • 27
    • 84889602565 scopus 로고    scopus 로고
    • Polymyxins and analogues bind to ribosomal RNA and interfere with eukaryotic translation in vitro
    • McCoy, L.S.; Robert, K.D.; Nation, R.L.; Thompson, P.E.; Velkov, T.; Li, J.; Tor, Y. Polymyxins and analogues bind to ribosomal RNA and interfere with eukaryotic translation in vitro. Chembiochem, 2013, 14, 2083-2086.
    • (2013) Chembiochem , vol.14 , pp. 2083-2086
    • McCoy, L.S.1    Robert, K.D.2    Nation, R.L.3    Thompson, P.E.4    Velkov, T.5    Li, J.6    Tor, Y.7
  • 28
    • 84868028125 scopus 로고    scopus 로고
    • Rapid killing of Acinetobacter baumannii by polymyxins is mediated by a hydroxyl radical death pathway. Antimicrob
    • Sampson, T.R.; Liu, X.; Schroeder, M.R.; Kraft, C.S.; Burd, E.M.; Weiss, D.S. Rapid killing of Acinetobacter baumannii by polymyxins is mediated by a hydroxyl radical death pathway. Antimicrob. Agents Chemother., 2012, 56, 5642-5649.
    • (2012) Agents Chemother. , vol.56 , pp. 5642-5649
    • Sampson, T.R.1    Liu, X.2    Schroeder, M.R.3    Kraft, C.S.4    Burd, E.M.5    Weiss, D.S.6
  • 29
    • 84908285941 scopus 로고    scopus 로고
    • Whole-animal chemical screen identifies colistin as a new immunomodulator that targets conserved pathways
    • Cai, Y.; Cao, X.; Aballay, A. Whole-animal chemical screen identifies colistin as a new immunomodulator that targets conserved pathways. MBio, 2014, 5, e01235-14.
    • (2014) Mbio , vol.5 , pp. e01235-e01314
    • Cai, Y.1    Cao, X.2    Aballay, A.3
  • 30
    • 77955846576 scopus 로고    scopus 로고
    • Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity
    • Takahashi, D.; Shukla, S.K.; Prakash, O.; Zhang, G. Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity. Biochimie, 2010, 92, 1236-1241.
    • (2010) Biochimie , vol.92 , pp. 1236-1241
    • Takahashi, D.1    Shukla, S.K.2    Prakash, O.3    Zhang, G.4
  • 31
    • 67649277613 scopus 로고    scopus 로고
    • Solution NMR studies of amphibian antimicrobial peptides: Linking structure to function?
    • Haney, E.F.; Hunter, H.N.; Matsuzaki, K.; Vogel, H.J. Solution NMR studies of amphibian antimicrobial peptides: Linking structure to function?. Biochim. Biophys. Acta, 2009, 1788, 1639-1655.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1639-1655
    • Haney, E.F.1    Hunter, H.N.2    Matsuzaki, K.3    Vogel, H.J.4
  • 32
    • 78651445030 scopus 로고    scopus 로고
    • Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents
    • Wiradharma, N.; Khoe, U.; Hauser, C.A.; Seow, S.V.; Zhang, S.; Yang, Y.Y. Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents. Biomaterials, 2011, 32, 2204-2212.
    • (2011) Biomaterials , vol.32 , pp. 2204-2212
    • Wiradharma, N.1    Khoe, U.2    Hauser, C.A.3    Seow, S.V.4    Zhang, S.5    Yang, Y.Y.6
  • 33
    • 34548233855 scopus 로고    scopus 로고
    • Synthetic lipopeptides: A novel class of anti-infectives
    • Jerala, R. Synthetic lipopeptides: a novel class of anti-infectives. Expert Opin. Investig. Drugs, 2007, 16, 1159-1169.
    • (2007) Expert Opin. Investig. Drugs , vol.16 , pp. 1159-1169
    • Jerala, R.1
  • 34
    • 84961702815 scopus 로고    scopus 로고
    • (Cubist Pharmaceuticals, Inc.) Novel lipopeptide antibacterial agents for the treatment of Gram positive infections. US Patent 20100184649 A1, July 22
    • Pearson, A.L.; Metcalf, C.A., III; Li, J. (Cubist Pharmaceuticals, Inc.) Novel lipopeptide antibacterial agents for the treatment of Gram positive infections. US Patent 20100184649 A1, July 22, 2010.
    • (2010)
    • Pearson, A.L.1    Metcalf, C.A.2    Li, J.3
  • 35
    • 84861163797 scopus 로고    scopus 로고
    • Activity of a novel cyclic lipopeptide, CB-183,315, against resistant Clostridium difficile and other Gram-positive aerobic and anaerobic intestinal pathogens. Antimicrob
    • Snydman, D.R.; Jacobus, N.V.; McDermott, L.A. Activity of a novel cyclic lipopeptide, CB-183,315, against resistant Clostridium difficile and other Gram-positive aerobic and anaerobic intestinal pathogens. Antimicrob. Agents Chemother., 2012, 56, 3448-3452.
    • (2012) Agents Chemother. , vol.56 , pp. 3448-3452
    • Snydman, D.R.1    Jacobus, N.V.2    McDermott, L.A.3
  • 36
    • 84903218446 scopus 로고    scopus 로고
    • Surotomycin demonstrates low in vitro frequency of resistance and rapid bactericidal activity in Clostridium difficile, Enterococcus faecalis, and Enterococcus faecium
    • Mascio, C.T.; Chesnel, L.; Thorne, G.; Silverman, J.A. Surotomycin demonstrates low in vitro frequency of resistance and rapid bactericidal activity in Clostridium difficile, Enterococcus faecalis, and Enterococcus faecium. Antimicrob. Agents Chemother., 2014, 58, 3976-3982.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 3976-3982
    • Mascio, C.T.1    Chesnel, L.2    Thorne, G.3    Silverman, J.A.4
  • 37
    • 84857768746 scopus 로고    scopus 로고
    • Daptomycin: A novel lipopeptide antibiotic against Gram-positive pathogens
    • Beiras-Fernandez, A.; Vogt, F.; Sodian, R.; Weis, F. Daptomycin: a novel lipopeptide antibiotic against Gram-positive pathogens. Infect. Drug Resist., 2010, 3, 95-101.
    • (2010) Infect. Drug Resist. , vol.3 , pp. 95-101
    • Beiras-Fernandez, A.1    Vogt, F.2    Sodian, R.3    Weis, F.4
  • 38
    • 84884949156 scopus 로고    scopus 로고
    • Current perspective on daptomycin for the clinical microbiologist
    • Humphries R.M.; Pollett, S.; Sakoulas, G. A current perspective on daptomycin for the clinical microbiologist. Clin. Microbiol. Rev., 2013, 26, 759-780.
    • (2013) Clin. Microbiol. Rev. , vol.26 , pp. 759-780
    • Humphries, R.M.1    Pollett, S.2    Sakoulas, G.A.3
  • 40
    • 71749100398 scopus 로고    scopus 로고
    • Cationic amphiphilic peptides with cancer-selective toxicity
    • Schweizer, F. Cationic amphiphilic peptides with cancer-selective toxicity. Eur. J. Pharmacol., 2009, 625, 190-194.
    • (2009) Eur. J. Pharmacol. , vol.625 , pp. 190-194
    • Schweizer, F.1
  • 42
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • Nguyen, L.T.; Haney, E.F.; Vogel, H.J. The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol., 2011, 29, 464-472.
    • (2011) Trends Biotechnol. , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 43
    • 83455200843 scopus 로고    scopus 로고
    • Effect of cholesterol on the membrane interaction of Modelin-5 isoforms
    • Dennison, S.R.; Phoenix, D.A. Effect of cholesterol on the membrane interaction of Modelin-5 isoforms. Biochemistry, 2011, 50, 10898-10909.
    • (2011) Biochemistry , vol.50 , pp. 10898-10909
    • Dennison, S.R.1    Phoenix, D.A.2
  • 44
    • 84865323371 scopus 로고    scopus 로고
    • Does cholesterol suppress the antimicrobial peptide induced disruption of lipid raft containing membranes
    • McHernry, A.J.; Sciacca, M.F.; Bremder, J.R.; Ramamoorthy, A. Does cholesterol suppress the antimicrobial peptide induced disruption of lipid raft containing membranes?. Biochim. Biophys. Acta, 2012, 1818, 3019-3024.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 3019-3024
    • McHernry, A.J.1    Sciacca, M.F.2    Bremder, J.R.3    Ramamoorthy, A.4
  • 45
    • 84878115669 scopus 로고    scopus 로고
    • Comparing bacterial membrane interactions and antimicrobial activity of porcine lactoferricin-derived peptides
    • Han, F.F.; Gao, Y.H.; Luan, C.; Xie, Y.G.; Liu, Y.F.; Wang, Y.Z. Comparing bacterial membrane interactions and antimicrobial activity of porcine lactoferricin-derived peptides. J. Dairy Sci., 2013, 96, 3471-3487.
    • (2013) J. Dairy Sci. , vol.96 , pp. 3471-3487
    • Han, F.F.1    Gao, Y.H.2    Luan, C.3    Xie, Y.G.4    Liu, Y.F.5    Wang, Y.Z.6
  • 47
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki, K.; Murase, O.; Fujii, N.; Miyajima, K. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry, 1996, 35, 11361-11368.
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 48
    • 0021905348 scopus 로고
    • Induction of autolysis of staphylococci by the basic peptide antibiotics Pep 5 and nisin and their influence on the activity of autolytic enzymes.
    • Bierbaum, G.; Sahl, H.G. Induction of autolysis of staphylococci by the basic peptide antibiotics Pep 5 and nisin and their influence on the activity of autolytic enzymes. Arch. Microbiol., 1985, 141, 249-254.
    • (1985) Arch. Microbiol. , vol.141 , pp. 249-254
    • Bierbaum, G.1    Sahl, H.G.2
  • 50
    • 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
  • 51
    • 79960936612 scopus 로고    scopus 로고
    • Multifunctional cationic host defence peptides and their clinical applications
    • Yeung, A.T.; Gellatly, S.L.; Hancock, R.E. Multifunctional cationic host defence peptides and their clinical applications. Cell. Mol. Life Sci., 2011, 68, 2161-2176.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2161-2176
    • Yeung, A.T.1    Gellatly, S.L.2    Hancock, R.E.3
  • 52
    • 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
  • 53
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and argininerich antimicrobial peptides: Structures and mechanisms of action
    • Chan, D.I.; Prenner, E.J.; Vogel, H.J. Tryptophan- and argininerich antimicrobial peptides: structures and mechanisms of action. Biochim. Biophys. Acta, 2006, 1758, 1184-1202.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 54
    • 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
  • 55
    • 0037443086 scopus 로고    scopus 로고
    • Interactions of the designed antimicrobial peptide MB21 and truncated dermaseptin S3 with lipid bilayers: Molecular-dynamics simulation
    • 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 simulation. 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
  • 56
    • 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    Maccallum, J.L.2    Tieleman, D.P.3
  • 57
    • 0028790095 scopus 로고
    • Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: Parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids
    • Kachel, K.; Asuncion-Punzalan, E.; London, E. Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids. Biochemistry, 1995, 34, 15475-15479.
    • (1995) Biochemistry , vol.34 , pp. 15475-15479
    • Kachel, K.1    Asuncion-Punzalan, E.2    London, E.3
  • 58
    • 0030043489 scopus 로고    scopus 로고
    • Cationi-pi interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D.A. Cationi-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science, 1996, 271, 163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 59
    • 0033544354 scopus 로고    scopus 로고
    • Cation-π interactions in proteins: Can simple models provide an accurate description
    • Minoux, H.; Chipot, C. Cation-π interactions in proteins: can simple models provide an accurate description? J. Am. Chem. Soc., 1999, 121, 10366-10372.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10366-10372
    • Minoux, H.1    Chipot, C.2
  • 60
    • 0028301445 scopus 로고
    • Amino/aromatic interactions in proteins: Is the evidence stacked against hydrogen bonding
    • Mitchell, J.B.; Nandi, C.L.; McDonald, I.K.; Thornton, J.M.; Price, S.L. Amino/aromatic interactions in proteins: is the evidence stacked against hydrogen bonding? J. Mol. Biol., 1994, 239, 315-331.
    • (1994) J. Mol. Biol. , vol.239 , pp. 315-331
    • Mitchell, J.B.1    Nandi, C.L.2    McDonald, I.K.3    Thornton, J.M.4    Price, S.L.5
  • 61
    • 0042060932 scopus 로고    scopus 로고
    • Conformation of bactericidal domain of puroindoline a: Structure and mechanism of action of a 13-residue antimicrobial peptide
    • Jing, W.; Demcoe, A.R.; Vogel, H.J. Conformation of bactericidal domain of puroindoline a: structure and mechanism of action of a 13-residue antimicrobial peptide. J. Bacteriol., 2003, 185, 4938-4947.
    • (2003) J. Bacteriol. , vol.185 , pp. 4938-4947
    • Jing, W.1    Demcoe, A.R.2    Vogel, H.J.3
  • 62
    • 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
  • 64
    • 79958756074 scopus 로고    scopus 로고
    • Studies on the lactoferricin-derived Escherichia coli membrane-active peptides reveal differences in the mechanism of N-acylated versus nonacylated peptides
    • Zweytick, D.; Deutsch, G.; Andra, J.; Blondelle, S.E.; Vollmer, E.; Jerala, R.; Lohner, K. Studies on the lactoferricin-derived Escherichia coli membrane-active peptides reveal differences in the mechanism of N-acylated versus nonacylated peptides. J. Biol. Chem., 2011, 286, 21266-21276.
    • (2011) J. Biol. Chem. , vol.286 , pp. 21266-21276
    • Zweytick, D.1    Deutsch, G.2    Andra, J.3    Blondelle, S.E.4    Vollmer, E.5    Jerala, R.6    Lohner, K.7
  • 65
    • 40849102416 scopus 로고    scopus 로고
    • Membrane curvature stress and antibacterial activity of lactoferricin derivatives
    • Zweytick, D.; Tumer, S.; Blondelle, S.E.; Lohner, K. Membrane curvature stress and antibacterial activity of lactoferricin derivatives. Biochem. Biophys. Res. Commun., 2008, 369, 395-400.
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 395-400
    • Zweytick, D.1    Tumer, S.2    Blondelle, S.E.3    Lohner, K.4
  • 66
    • 0347766076 scopus 로고    scopus 로고
    • The effects of shortening lactoferrin dereived peptides against tumour cells, bacteria and normal human cells
    • Yang, N.; Strøm, M.B.; Mekonnen, S.M; Svendsen, J.S.; Rekdal, O. The effects of shortening lactoferrin dereived peptides against tumour cells, bacteria and normal human cells. J. Pept. Sci., 2004, 10, 37-46.
    • (2004) J. Pept. Sci. , vol.10 , pp. 37-46
    • Yang, N.1    Strøm, M.B.2    Mekonnen, S.M.3    Svendsen, J.S.4    Rekdal, O.5
  • 67
    • 0029867221 scopus 로고    scopus 로고
    • Synthetic combinatorial libraries: Novel discovery strategy for identification of antimicrobial agents. Antimicrob
    • Blondelle, S.E.; Pérez-Payá, E.; Houghten R.A. Synthetic combinatorial libraries: novel discovery strategy for identification of antimicrobial agents. Antimicrob. Agents Chemother., 1996, 40, 1067-1071.
    • (1996) Agents Chemother. , vol.40 , pp. 1067-1071
    • Blondelle, S.E.1    Pérez-Payá, E.2    Houghten, R.A.3
  • 68
    • 0038064549 scopus 로고    scopus 로고
    • Antimicrobial activity of short arginine- and tryptophan-rich peptides
    • Strøm, M.B.; Rekdal, O.; Svendsen J.S. Antimicrobial activity of short arginine- and tryptophan-rich peptides. J. Pept. Sci., 2002, 8, 431-437.
    • (2002) J. Pept. Sci. , vol.8 , pp. 431-437
    • Strøm, M.B.1    Rekdal, O.2    Svendsen, J.S.3
  • 69
    • 0026419319 scopus 로고
    • Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery
    • Houghten, R.A.; Pinilla, C.; Blondelle, S.E.; Appel, J.R.; Dooley, C.T.; Cuervo, J.H. Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery. Nature, 1991, 354, 84-86.
    • (1991) Nature , vol.354 , pp. 84-86
    • Houghten, R.A.1    Pinilla, C.2    Blondelle, S.E.3    Appel, J.R.4    Dooley, C.T.5    Cuervo, J.H.6
  • 70
    • 33644926727 scopus 로고    scopus 로고
    • Solution structure of a novel tryptophan-rich peptide with bidirectional antimicrobial activity
    • Wei, S.Y.; Wu, J.M.; Kuo, Y.Y.; Chen, H.L.; Yip, B.S.; Tzeng, S.R.; Cheng, J.W. Solution structure of a novel tryptophan-rich peptide with bidirectional antimicrobial activity. J. Bacteriol., 2006, 188, 328-334.
    • (2006) J. Bacteriol. , vol.188 , pp. 328-334
    • Wei, S.Y.1    Wu, J.M.2    Kuo, Y.Y.3    Chen, H.L.4    Yip, B.S.5    Tzeng, S.R.6    Cheng, J.W.7
  • 74
    • 84867790397 scopus 로고    scopus 로고
    • Modulating the activity of short arginine-tryptophan containing antibacterial peptides with Nterminal metallocenoyl groups
    • Albada, H.B.; Chiriac, A.I.; Wenzel, M.; Penkova, M.; Bandow, J.E.; Sahl, H.G.; Metzler-Nolte, N. Modulating the activity of short arginine-tryptophan containing antibacterial peptides with Nterminal metallocenoyl groups. Beilstein J. Org. Chem., 2012, 8, 1753-1764.
    • (2012) Beilstein J. Org. Chem. , vol.8 , pp. 1753-1764
    • Albada, H.B.1    Chiriac, A.I.2    Wenzel, M.3    Penkova, M.4    Bandow, J.E.5    Sahl, H.G.6    Metzler-Nolte, N.7
  • 76
    • 84887597873 scopus 로고    scopus 로고
    • Short antibacterial peptides with significantly reduced hemolytic activity can be identified by a systematid L-to-D exchance scan of their amino acid residues
    • Albada, H.B.; Prochnow, P.; Bobersky, S.; Langklotz, S.; Bandow, J.E.; Metzler-Nolte, N. Short antibacterial peptides with significantly reduced hemolytic activity can be identified by a systematid L-to-D exchance scan of their amino acid residues. ACS Comb. Sci., 2013, 15, 585-592.
    • (2013) ACS Comb. Sci. , vol.15 , pp. 585-592
    • Albada, H.B.1    Prochnow, P.2    Bobersky, S.3    Langklotz, S.4    Bandow, J.E.5    Metzler-Nolte, N.6
  • 77
    • 84888046119 scopus 로고    scopus 로고
    • Design of short membrane selective antimicrobial peptides containing tryptophan and arginine residues for improved activity, salt-resistance, and biocompatibility
    • Saravanan, R.; Li, X.; Lim, K.; Mohanram, H.; Peng, L.; Mishra, B.; Basu, A.; Lee, J.M.; Bhattacharjya, S.; Leong, S.S. Design of short membrane selective antimicrobial peptides containing tryptophan and arginine residues for improved activity, salt-resistance, and biocompatibility. Biotechnol. Bioeng., 2014, 111, 37-49.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 37-49
    • Saravanan, R.1    Li, X.2    Lim, K.3    Mohanram, H.4    Peng, L.5    Mishra, B.6    Basu, A.7    Lee, J.M.8    Bhattacharjya, S.9    Leong, S.S.10
  • 79
    • 84902649528 scopus 로고    scopus 로고
    • Tuning the antimicrobial pharmacophore to enable discovery of short lipopeptides with multiple modes of action
    • Fang, Y.; Zhong, W.; Wang, Y.; Xun, T.; Lin, D.; Liu, W.; Wang, J.; Lv, L.; Liu, S.; He, J. Tuning the antimicrobial pharmacophore to enable discovery of short lipopeptides with multiple modes of action. Eur. J. Med. Chem., 2014, 18, 36-44.
    • (2014) Eur. J. Med. Chem. , vol.18 , pp. 36-44
    • Fang, Y.1    Zhong, W.2    Wang, Y.3    Xun, T.4    Lin, D.5    Liu, W.6    Wang, J.7    Lv, L.8    Liu, S.9    He, J.10
  • 80
    • 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
  • 81
    • 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
  • 83
    • 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
  • 84
    • 0036633301 scopus 로고    scopus 로고
    • The short proline-rich antibacterial peptide family
    • Otvos, L. Jr. The short proline-rich antibacterial peptide family. Cell. Mol. Life Sci., 2002, 59, 1138-1150.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1138-1150
    • Otvos, L.1
  • 85
    • 9144258550 scopus 로고    scopus 로고
    • Antibacterial proline-rich oligopeptides and their target proteins
    • Markossian, K.A.; Zamyatnin, A.A.; Kurganov, B.I. Antibacterial proline-rich oligopeptides and their target proteins. Biochemistry (Mosc.), 2004, 69, 1082-1091.
    • (2004) Biochemistry (Mosc.) , vol.69 , pp. 1082-1091
    • Markossian, K.A.1    Zamyatnin, A.A.2    Kurganov, B.I.3
  • 88
    • 0035700551 scopus 로고    scopus 로고
    • Tripropeptins, novel antimicrobial agents produced by Lysobacter sp. I. Taxonomy, isolation and biological activities
    • Hashizume, H.; Igarashi, M.; Hattori, S.; Hori, M.; Hamada, M.; Takeuchi, T. Tripropeptins, novel antimicrobial agents produced by Lysobacter sp. I. Taxonomy, isolation and biological activities. J. Antibiot., (Tokyo), 2001, 54, 1054-1059.
    • (2001) J. Antibiot., (Tokyo) , vol.54 , pp. 1054-1059
    • Hashizume, H.1    Igarashi, M.2    Hattori, S.3    Hori, M.4    Hamada, M.5    Takeuchi, T.6
  • 89
    • 3242889733 scopus 로고    scopus 로고
    • Tripropeptin E, a new tripropeptin group antibiotic produced by Lysobacter sp. BMK333-48F3
    • Hashizume, H.; Hattori, S.; Igarashi, M.; Akamatsu, Y. Tripropeptin E, a new tripropeptin group antibiotic produced by Lysobacter sp. BMK333-48F3. J. Antibiot. (Tokyo), 2004, 57, 394-399.
    • (2004) J. Antibiot. (Tokyo) , vol.57 , pp. 394-399
    • Hashizume, H.1    Hattori, S.2    Igarashi, M.3    Akamatsu, Y.4
  • 90
    • 57849165933 scopus 로고    scopus 로고
    • New type of tripropeptin with anteiso-branched chain fatty acid from Lysobacter sp. BMK333-48F3
    • Hashizume, H.; Igarashi, M.; Sawa, R.; Adachi, H.; Nishimura, Y.; Akamatsu, Y. A new type of tripropeptin with anteiso-branched chain fatty acid from Lysobacter sp. BMK333-48F3. J. Antibiot. (Tokyo), 2008, 61, 577-582.
    • (2008) J. Antibiot. (Tokyo) , vol.61 , pp. 577-582
    • Hashizume, H.1    Igarashi, M.2    Sawa, R.3    Adachi, H.4    Nishimura, Y.5    Akamatsu, Y.A.6
  • 92
    • 0034999983 scopus 로고    scopus 로고
    • Katanosin B and plusbacin A(3), inhibitors of peptidoglycan synthesis in methicillin-resistant Staphylococcus aureus
    • Maki, H.; Miura, K.; Yamano, Y. Katanosin B and plusbacin A(3), inhibitors of peptidoglycan synthesis in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother., 2001, 45, 1823-1827.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1823-1827
    • Maki, H.1    Miura, K.2    Yamano, Y.3
  • 93
    • 77956947687 scopus 로고    scopus 로고
    • Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP
    • Li, D.H.; Chung, Y.S.; Gloyd, M.; Joseph, E.; Ghirlando, R.; Wright, G.D.; Cheng, Y.Q.; Maurizi, M.R.; Guarne, A.; Ortega, J. Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP. Chem. Biol., 2010, 17, 959-969.
    • (2010) Chem. Biol. , vol.17 , pp. 959-969
    • Li, D.H.1    Chung, Y.S.2    Gloyd, M.3    Joseph, E.4    Ghirlando, R.5    Wright, G.D.6    Cheng, Y.Q.7    Maurizi, M.R.8    Guarne, A.9    Ortega, J.10
  • 95
    • 84961712813 scopus 로고
    • A54556 antibiotics and process for production thereof. US Patent 4492650 A, January 8
    • Michel, K.H.; Kastner, R.E. A54556 antibiotics and process for production thereof. US Patent 4492650 A, January 8, 1985.
    • (1985)
    • Michel, K.H.1    Kastner, R.E.2
  • 96
    • 0026351941 scopus 로고
    • Enopeptin A, a novel depsipeptide
    • Osada, H.; Yano, T.; Koshino, H.; Isono, K. Enopeptin A, a novel depsipeptide antibiotic with anti-bacteriophage activity. J. Antiobiot. (Tokyo), 1991, 44, 1463-1466.
    • (1991) J. Antiobiot. (Tokyo) , vol.44 , pp. 1463-1466
    • Osada, H.1    Yano, T.2    Koshino, H.3    Isono, K.4
  • 98
    • 77957570418 scopus 로고    scopus 로고
    • Diversityoriented synthesis of cyclic acyldepsipeptides leads to the discovery of a potent antibacterial agent. Bioorg. Med
    • Socha, A.M.; Tan, N.Y.; LaPlante, K.L.; Sello, J.K. Diversityoriented synthesis of cyclic acyldepsipeptides leads to the discovery of a potent antibacterial agent. Bioorg. Med. Chem., 2010, 18, 7193-7202.
    • (2010) Chem. , vol.18 , pp. 7193-7202
    • Socha, A.M.1    Tan, N.Y.2    Laplante, K.L.3    Sello, J.K.4
  • 99
    • 84893790296 scopus 로고    scopus 로고
    • Restriction of the conformational dynamics of the cyclic acyldepsipeptide antibiotics improves their antibacterial activity
    • Carney, D.W.; Schmitz, K.R.; Truong, J.V.; Sauer, R.T.; Sello, J.K. Restriction of the conformational dynamics of the cyclic acyldepsipeptide antibiotics improves their antibacterial activity. J. Am. Chem. Soc., 2014, 136, 1922-1929.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 1922-1929
    • Carney, D.W.1    Schmitz, K.R.2    Truong, J.V.3    Sauer, R.T.4    Sello, J.K.5
  • 100
    • 33846446696 scopus 로고    scopus 로고
    • Cyclic heptapeptides from the Jamaican sponge Stylissa caribica
    • Mohammed, R.; Peng, J.; Kelly, M.; Hamann, M.T. Cyclic heptapeptides from the Jamaican sponge Stylissa caribica. J. Nat. Prod., 2006, 69, 1739-1744.
    • (2006) J. Nat. Prod. , vol.69 , pp. 1739-1744
    • Mohammed, R.1    Peng, J.2    Kelly, M.3    Hamann, M.T.4
  • 101
    • 61449176998 scopus 로고    scopus 로고
    • Synthesis, cytotoxic and antimicrobial screeningof a proline-rich cyclopolypeptide
    • Dahiya, R.; Kumar, A.; Gupta, R. Synthesis, cytotoxic and antimicrobial screening of a proline-rich cyclopolypeptide. Chem. Pharm. Bull. (Tokyo), 2009, 57, 214-217.
    • (2009) Chem. Pharm. Bull. (Tokyo) , vol.57 , pp. 214-217
    • Dahiya, R.1    Kumar, A.2    Gupta, R.3
  • 102
    • 77956397625 scopus 로고    scopus 로고
    • Total synthesis and antimicrobial activity of a natural cycloheptapeptide of marine origin
    • Dahiya, R.; Gautam, H. Total synthesis and antimicrobial activity of a natural cycloheptapeptide of marine origin. Mar. Drugs, 2010, 8, 2384-2394.
    • (2010) Mar. Drugs , vol.8 , pp. 2384-2394
    • Dahiya, R.1    Gautam, H.2
  • 103
    • 0021164005 scopus 로고
    • Empedopeptin (BMY-28117), a new depsipeptide antibiotic. II. Structure determination
    • Sugawara, K.; Numata, K.; Konishi, M.; Kawaguchi H. Empedopeptin (BMY-28117), a new depsipeptide antibiotic. II. Structure determination. J. Antibiot. (Tokyo), 1984, 37, 958-964.
    • (1984) J. Antibiot. (Tokyo) , vol.37 , pp. 958-964
    • Sugawara, K.1    Numata, K.2    Konishi, M.3    Kawaguchi, H.4
  • 106
    • 84899441126 scopus 로고    scopus 로고
    • Purification, structural elucidation and bioactivity of tryptophan containing diketopiperazines, from Comamonas testosterone associated with a rhabditid entomopathogenic nematode against major humanpathogenic bacteria
    • Kumar, S.N.; Mohandas, C.; Nambisan, B. Purification, structural elucidation and bioactivity of tryptophan containing diketopiperazines, from Comamonas testosterone associated with a rhabditid entomopathogenic nematode against major humanpathogenic bacteria. Peptides, 2014, 53, 48-58.
    • (2014) Peptides , vol.53 , pp. 48-58
    • Kumar, S.N.1    Mohandas, C.2    Nambisan, B.3
  • 107
    • 46249092608 scopus 로고    scopus 로고
    • Antibacterial hydrogels of amino acid-based cationic amphiphiles
    • Roy, S.; Das, P.K. Antibacterial hydrogels of amino acid-based cationic amphiphiles. Biotechnol. Bioeng., 2008, 100, 756-764.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 756-764
    • Roy, S.1    Das, P.K.2
  • 108
    • 57549084478 scopus 로고    scopus 로고
    • Antimicrobial activity, biocompatibility and hydrogelation ability of dipeptide-based amphiphiles
    • Mitra, R.N.; Shome, A.; Paul, P.; Das, P.K. Antimicrobial activity, biocompatibility and hydrogelation ability of dipeptide-based amphiphiles. Org. Biomol. Chem., 2009, 7, 94-102.
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 94-102
    • Mitra, R.N.1    Shome, A.2    Paul, P.3    Das, P.K.4
  • 109
    • 33750446295 scopus 로고    scopus 로고
    • Ultrashort antibacterial and antifungal lipopeptides
    • Makovitzki, A.; Avrahami, D.; Shai, Y. Ultrashort antibacterial and antifungal lipopeptides. Proc. Natl. Acad. U.S.A., 2006, 103, 15997-16002.
    • (2006) Proc. Natl. Acad. U.S.A. , vol.103 , pp. 15997-16002
    • Makovitzki, A.1    Avrahami, D.2    Shai, Y.3
  • 110
    • 84873497595 scopus 로고    scopus 로고
    • Ultrashort cationic lipopeptides and lipopeptoids selectively induced cytokine production in macrophages
    • e54280
    • Findlay, B.; Mookherjee, N.; Schweizer, F. Ultrashort cationic lipopeptides and lipopeptoids selectively induced cytokine production in macrophages. PLoS One, 2013, 8, e54280.
    • (2013) Plos One , pp. 8
    • Findlay, B.1    Mookherjee, N.2    Schweizer, F.3
  • 111
    • 66149142186 scopus 로고    scopus 로고
    • Antibacterial activity of ultrashort cationic lipo-beta-peptides. Antimicrob
    • Serrano, G.N.; Zhanel, G.G.; Schweizer, F. Antibacterial activity of ultrashort cationic lipo-beta-peptides. Antimicrob. Agents Chemother., 2009, 53, 2214-2217.
    • (2009) Agents Chemother. , vol.53 , pp. 2214-2217
    • Serrano, G.N.1    Zhanel, G.G.2    Schweizer, F.3
  • 112
    • 84861875478 scopus 로고    scopus 로고
    • Investigating the antimicrobial peptide ‘window of activity’ using cationic lipopeptides with hydrocarbon and fluorinated tails
    • Findlay, B.; Zhanel, G.G.; Schweizer, F. Investigating the antimicrobial peptide ‘window of activity’ using cationic lipopeptides with hydrocarbon and fluorinated tails. Int. J. Antimicrob. Agents, 2012, 40, 36-42.
    • (2012) Int. J. Antimicrob. Agents , vol.40 , pp. 36-42
    • Findlay, B.1    Zhanel, G.G.2    Schweizer, F.3
  • 113
    • 84933517638 scopus 로고    scopus 로고
    • Structure-activity relationships in ultrashort cationic lipopeptides: The effects of amino acid ring constraint on antibacterial activity
    • Domalaon, R.; Yang, X.; O’Neil, J.; Zhanel, G.G.; Mookherjee, N.; Schweizer F. Structure-activity relationships in ultrashort cationic lipopeptides: the effects of amino acid ring constraint on antibacterial activity. Amino Acids, 2014, 46, 2517-2530.
    • (2014) Amino Acids , vol.46 , pp. 2517-2530
    • Domalaon, R.1    Yang, X.2    O’Neil, J.3    Zhanel, G.G.4    Mookherjee, N.5    Schweizer, F.6
  • 115
    • 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
  • 116
    • 84904824145 scopus 로고    scopus 로고
    • Design and synthesis of membranetargeting antibiotics: From peptides- to aminosugar-based antimicrobial cationic amphiphiles
    • Herzog, I.M.; Fridman, M. Design and synthesis of membranetargeting antibiotics: from peptides- to aminosugar-based antimicrobial cationic amphiphiles. Med. Chem. Commun., 2014, 5, 1014-1026.
    • (2014) Med. Chem. Commun. , vol.5 , pp. 1014-1026
    • Herzog, I.M.1    Fridman, M.2
  • 118
    • 84871395889 scopus 로고    scopus 로고
    • Peptide scanning for studying structure-activity relationships in drug discovery
    • Jamieson, A.G.; Boutard, N.; Sabatino, D.; Lubell, W.D. Peptide scanning for studying structure-activity relationships in drug discovery. Chem. Biol. Drug Des., 2013, 81, 148-165.
    • (2013) Chem. Biol. Drug Des. , vol.81 , pp. 148-165
    • Jamieson, A.G.1    Boutard, N.2    Sabatino, D.3    Lubell, W.D.4
  • 120
    • 84907879304 scopus 로고    scopus 로고
    • Peptidomimetics as a new generation of antimicrobial agents: Current progress
    • Méndez-Samperio, P. Peptidomimetics as a new generation of antimicrobial agents: current progress. Infect. Drug Resist., 2014, 7, 229-237.
    • (2014) Infect. Drug Resist. , vol.7 , pp. 229-237
    • Méndez-Samperio, P.1
  • 121
    • 77957329669 scopus 로고    scopus 로고
    • Cationic amphiphilies, a new generation of antimicrobials inspired by the natural antimicrobial peptide scaffold. Antimicrob
    • Findlay, B.; Zhanel, G.G.; Schweizer, F. Cationic amphiphilies, a new generation of antimicrobials inspired by the natural antimicrobial peptide scaffold. Antimicrob. Agents Chemother., 2010, 54, 4049-4058.
    • (2010) Agents Chemother. , vol.54 , pp. 4049-4058
    • Findlay, B.1    Zhanel, G.G.2    Schweizer, F.3
  • 122
    • 84866943640 scopus 로고    scopus 로고
    • Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: A comparative study of different backbones
    • Jahnsen, R.D.; Frimodt-Møller, 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-Møller, N.2    Franzyk, H.3
  • 123
    • 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
  • 126
    • 3843109179 scopus 로고    scopus 로고
    • Bulky nonproteinogenic amino acids permit the design of very small and effective cationic antibacterial peptides
    • Haug, B.E.; Stensen, W.; Stiberg, T.; Svendsen, J.S. Bulky nonproteinogenic amino acids permit the design of very small and effective cationic antibacterial peptides. J. Med. Chem., 2004, 47, 4159-4162.
    • (2004) J. Med. Chem. , vol.47 , pp. 4159-4162
    • Haug, B.E.1    Stensen, W.2    Stiberg, T.3    Svendsen, J.S.4
  • 127
    • 33947586139 scopus 로고    scopus 로고
    • Application of the Suzuki- Miyaura cross-coupling to increase antimicrobial potency generates promising novel antibacterials.
    • Haug, B.E.; Stensen, W.; Svendsen, J.S. Application of the Suzuki- Miyaura cross-coupling to increase antimicrobial potency generates promising novel antibacterials. Bioorg. Med. Chem. Lett., 2007, 17, 2361-2364.
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , pp. 2361-2364
    • Haug, B.E.1    Stensen, W.2    Svendsen, J.S.3
  • 128
    • 47749116861 scopus 로고    scopus 로고
    • Synthetic antimicrobial peptidomimetics with therapeutic potention
    • Haug, B.E.; Stensen, W.; Kalaaji, M.; Rekdal, O.; Svendsen, J.S. Synthetic antimicrobial peptidomimetics with therapeutic potention. J. Med. Chem., 2008, 51, 4306-4314.
    • (2008) J. Med. Chem. , vol.51 , pp. 4306-4314
    • Haug, B.E.1    Stensen, W.2    Kalaaji, M.3    Rekdal, O.4    Svendsen, J.S.5
  • 129
    • 84864381356 scopus 로고    scopus 로고
    • In vitro activities of LTX-109, a synthetic antimicrobial peptide, against methicillinresistant, vancomycin-intermediate, vancomycin-resistant, daptomycin- nonsusceptible, and linezolid-nonsusceptible Staphylococcus aureus
    • Saravolatz, L.D.; Pawlak, J.; Johnson, L.; Bonilla, H.; Saravolatz L.D. 2nd.; Fakih, M.G.; Fugelli, A.; Olsen, W.M. In vitro activities of LTX-109, a synthetic antimicrobial peptide, against methicillinresistant, vancomycin-intermediate, vancomycin-resistant, daptomycin- nonsusceptible, and linezolid-nonsusceptible Staphylococcus aureus. Antimicrob. Agents Chemother., 2012, 56, 4478-4482.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 4478-4482
    • Saravolatz, L.D.1    Pawlak, J.2    Johnson, L.3    Bonilla, H.4    Saravolatz, L.D.5    Fakih, M.G.6    Fugelli, A.7    Olsen, W.M.8
  • 130
    • 80051860378 scopus 로고    scopus 로고
    • A synthetic antimicrobial peptidomimetic (LTX 109): Stereochemical impact on membrane disruption
    • Isaksson, J.; Brandsdal, B.O.; Enggvist, M.; Flaten, G.E.; Svendsen, J.S.; Stensen, W. A synthetic antimicrobial peptidomimetic (LTX 109): stereochemical impact on membrane disruption. J. Med. Chem., 2011, 54, 5786-5795.
    • (2011) J. Med. Chem. , vol.54 , pp. 5786-5795
    • Isaksson, J.1    Brandsdal, B.O.2    Enggvist, M.3    Flaten, G.E.4    Svendsen, J.S.5    Stensen, W.6
  • 134
    • 84906081308 scopus 로고    scopus 로고
    • Comparative mechanistic studies of brilacidin, daptomycin, and the antimicrobial peptide LL16
    • Mensa, B.; Howell, G.L.; Scott, R.; De Grado, W.F. Comparative mechanistic studies of brilacidin, daptomycin, and the antimicrobial peptide LL16. Antimicrob. Agents Chemother., 2014, 58, 5136-5145.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 5136-5145
    • Mensa, B.1    Howell, G.L.2    Scott, R.3    De Grado, W.F.4
  • 135
    • 54049134708 scopus 로고    scopus 로고
    • The design, structures and therapeutic potential of protein epitope mimetics
    • Robinson, J.A.; Demarco, S.; Gombert, F.; Moehle, K.; Obrecht, D. The design, structures and therapeutic potential of protein epitope mimetics. Drug Discov. Today, 2008, 13, 944-951.
    • (2008) Drug Discov. Today , vol.13 , pp. 944-951
    • Robinson, J.A.1    Demarco, S.2    Gombert, F.3    Moehle, K.4    Obrecht, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.