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Volumn 6, Issue 12, 2013, Pages 1543-1575

Antimicrobial peptides

Author keywords

Antimicrobial peptide; Biofilm; Persister

Indexed keywords

AMPICILLIN; ANTIBIOTIC AGENT; ANTIFUNGAL AGENT; ANTIPARASITIC AGENT; ANTIVIRUS AGENT; LACTICIN Q; NISIN; NISIN A; NP 1 PEPTIDE; PEDIOCIN; PENICILLIN DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 84888632051     PISSN: None     EISSN: 14248247     Source Type: Journal    
DOI: 10.3390/ph6121543     Document Type: Review
Times cited : (1082)

References (239)
  • 1
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown, K.L.; Hancock, R.E. Cationic host defense (antimicrobial) peptides. Curr. Opin. Immunol. 2006, 18, 24-30.
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 2
  • 3
    • 0032821714 scopus 로고    scopus 로고
    • Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens
    • Groenink, J.; Walgreen-Weterings, E.; van't Hof, W.; Veerman, E.C.; Nieuw Amerongen, A.V. Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens. FEMS Microbiol. Lett. 1999, 179, 217-222.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 217-222
    • Groenink, J.1    Walgreen-Weterings, E.2    van't Hof, W.3    Veerman, E.C.4    Nieuw Amerongen, A.V.5
  • 4
    • 0042734451 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides: Issues for potential clinical use
    • Bradshaw, J. Cationic antimicrobial peptides: Issues for potential clinical use. BioDrugs 2003, 17, 233-240.
    • (2003) BioDrugs , vol.17 , pp. 233-240
    • Bradshaw, J.1
  • 5
    • 80053440806 scopus 로고    scopus 로고
    • Membrane-active host defense peptides-challenges and perspectives for the development of novel anticancer drugs
    • Riedl, S.; Zweytick, D.; Lohner, K. Membrane-active host defense peptides-challenges and perspectives for the development of novel anticancer drugs. Chem. Phys. Lipids 2011, 164, 766-781.
    • (2011) Chem. Phys. Lipids , vol.164 , pp. 766-781
    • Riedl, S.1    Zweytick, D.2    Lohner, K.3
  • 6
    • 79953148897 scopus 로고    scopus 로고
    • Alpha-helical cationic antimicrobial peptides: Relationships of structure and function
    • Huang, Y.B.; Huang, J.F.; Chen, Y.X. Alpha-helical cationic antimicrobial peptides: Relationships of structure and function. Protein Cell 2010, 1, 143-152.
    • (2010) Protein Cell , vol.1 , pp. 143-152
    • Huang, Y.B.1    Huang, J.F.2    Chen, Y.X.3
  • 7
    • 85024321592 scopus 로고
    • Studies on a bactericidal agent extracted from a soil bacillus: I. Preparation of the agent. Its activity in vitro
    • Dubos, R.J. Studies on a bactericidal agent extracted from a soil bacillus: I. Preparation of the agent. Its activity in vitro. J. Exp. Med. 1939, 70, 1-10.
    • (1939) J. Exp. Med. , vol.70 , pp. 1-10
    • Dubos, R.J.1
  • 8
    • 85025377717 scopus 로고
    • Studies on a bactericidal agent extracted from a soil bacillus: II. Protective effect of the bactericidal agent against experimental Pneumococcus infections in mice
    • Dubos, R.J. Studies on a bactericidal agent extracted from a soil bacillus: II. Protective effect of the bactericidal agent against experimental Pneumococcus infections in mice. J. Exp. Med. 1939, 70, 11-17.
    • (1939) J. Exp. Med. , vol.70 , pp. 11-17
    • Dubos, R.J.1
  • 9
    • 0001546676 scopus 로고
    • Fractionation of the bactericidal agent from cultures of a soil Bacillus
    • Hotchkiss, R.D.; Dubos, R.J. Fractionation of the bactericidal agent from cultures of a soil Bacillus. J. Biol. Chem. 1940, 132, 791-792.
    • (1940) J. Biol. Chem. , vol.132 , pp. 791-792
    • Hotchkiss, R.D.1    Dubos, R.J.2
  • 10
    • 33645419340 scopus 로고    scopus 로고
    • Rene dubos: Unearthing antibiotics
    • Van Epps, H.L. Rene dubos: Unearthing antibiotics. J. Exp. Med. 2006, 203, 259.
    • (2006) J. Exp. Med. , vol.203 , pp. 259
    • Van Epps, H.L.1
  • 11
    • 85025407868 scopus 로고
    • The production of bactericidal substances by aerobic sporulating bacilli
    • Dubos, R.J.; Hotchkiss, R.D. The production of bactericidal substances by aerobic sporulating bacilli. J. Exp. Med. 1941, 73, 629-640.
    • (1941) J. Exp. Med. , vol.73 , pp. 629-640
    • Dubos, R.J.1    Hotchkiss, R.D.2
  • 12
    • 84877352370 scopus 로고
    • Toxic effects of tyrothricin, gramicidin and tyrocidine
    • Rammelkamp, C.H.; Weinstein, L. Toxic effects of tyrothricin, gramicidin and tyrocidine. J. Infect. Dis. 1942, 71, 166-173.
    • (1942) J. Infect. Dis. , vol.71 , pp. 166-173
    • Rammelkamp, C.H.1    Weinstein, L.2
  • 13
    • 0001131393 scopus 로고
    • A crystalline protein obtained from a lipoprotein of wheat flour
    • Balls, A.K. A crystalline protein obtained from a lipoprotein of wheat flour. Cereal Chem. 1942, 19, 279-288.
    • (1942) Cereal Chem. , vol.19 , pp. 279-288
    • Balls, A.K.1
  • 14
    • 0017396536 scopus 로고
    • Complete primary structures of two subunits of purothionin a, a lethal protein for brewer's yeast from wheat flour
    • Ohtani, S.; Okada, T.; Yoshizumi, H.; Kagamiyama, H. Complete primary structures of two subunits of purothionin a, a lethal protein for brewer's yeast from wheat flour. J. Biochem. 1977, 82, 753-767.
    • (1977) J. Biochem. , vol.82 , pp. 753-767
    • Ohtani, S.1    Okada, T.2    Yoshizumi, H.3    Kagamiyama, H.4
  • 15
    • 0000617857 scopus 로고
    • Phagocytin: A bactericidal substance from polymorphonuclear leucocytes
    • Hirsch, J.G. Phagocytin: A bactericidal substance from polymorphonuclear leucocytes. J. Exp. Med. 1956, 103, 589-611.
    • (1956) J. Exp. Med. , vol.103 , pp. 589-611
    • Hirsch, J.G.1
  • 16
    • 50549170868 scopus 로고
    • Uber das giftsekret der gelbbauchunke, Bombina variegata L
    • Kiss, G.; Michl, H. Uber das giftsekret der gelbbauchunke, Bombina variegata L. Toxicon 1962, 1, 33-34.
    • (1962) Toxicon , vol.1 , pp. 33-34
    • Kiss, G.1    Michl, H.2
  • 17
    • 0013855162 scopus 로고
    • Poliomorphism in the red protein isolated from milk of individual cows
    • Groves, M.L.; Peterson, R.F.; Kiddy, C.A. Poliomorphism in the red protein isolated from milk of individual cows. Nature 1965, 207, 1007-1008.
    • (1965) Nature , vol.207 , pp. 1007-1008
    • Groves, M.L.1    Peterson, R.F.2    Kiddy, C.A.3
  • 18
    • 0000255408 scopus 로고
    • Antibacterial and enzymic basic proteins from leukocyte lysosomes: Separation and identification
    • Zeya, H.I.; Spitznagel, J.K. Antibacterial and enzymic basic proteins from leukocyte lysosomes: Separation and identification. Science 1963, 142, 1085-1087.
    • (1963) Science , vol.142 , pp. 1085-1087
    • Zeya, H.I.1    Spitznagel, J.K.2
  • 19
    • 84879184644 scopus 로고    scopus 로고
    • Lamp: A database linking antimicrobial peptides
    • Zhao, X.; Wu, H.; Lu, H.; Li, G.; Huang, Q. Lamp: A database linking antimicrobial peptides. PLoS One 2013, 8, e66557.
    • (2013) PLoS One , vol.8
    • Zhao, X.1    Wu, H.2    Lu, H.3    Li, G.4    Huang, Q.5
  • 20
    • 77950471557 scopus 로고    scopus 로고
    • Antimicrobial peptides in frog skin secretions
    • Conlon, J.M.; Sonnevend, A. Antimicrobial peptides in frog skin secretions. Methods Mol. Biol. 2010, 618, 3-14.
    • (2010) Methods Mol. Biol. , vol.618 , pp. 3-14
    • Conlon, J.M.1    Sonnevend, A.2
  • 21
    • 34748844591 scopus 로고    scopus 로고
    • Antimicrobial peptides: Natural effectors of the innate immune system
    • Radek, K.; Gallo, R. Antimicrobial peptides: Natural effectors of the innate immune system. Semin. Immunopathol. 2007, 29, 27-43.
    • (2007) Semin. Immunopathol. , vol.29 , pp. 27-43
    • Radek, K.1    Gallo, R.2
  • 22
    • 78449236736 scopus 로고    scopus 로고
    • Antimicrobial peptides: Primeval molecules or future drugs?
    • Peters, B.M.; Shirtliff, M.E.; Jabra-Rizk, M.A. Antimicrobial peptides: Primeval molecules or future drugs? PLoS Pathog. 2010, 6, e1001067.
    • (2010) PLoS Pathog. , vol.6
    • Peters, B.M.1    Shirtliff, M.E.2    Jabra-Rizk, M.A.3
  • 23
    • 0032993170 scopus 로고    scopus 로고
    • Antimicrobial and cytolytic polypeptides of amoeboid protozoa-Effector molecules of primitive phagocytes
    • Leippe, M. Antimicrobial and cytolytic polypeptides of amoeboid protozoa-Effector molecules of primitive phagocytes. Dev. Comp. Immunol. 1999, 23, 267-279.
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 267-279
    • Leippe, M.1
  • 24
    • 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
  • 25
    • 48349087831 scopus 로고    scopus 로고
    • Antimicrobial peptides and the skin immune defense system
    • Schauber, J.; Gallo, R.L. Antimicrobial peptides and the skin immune defense system. J. Allergy Clin. Immunol. 2008, 122, 261-266.
    • (2008) J. Allergy Clin. Immunol. , vol.122 , pp. 261-266
    • Schauber, J.1    Gallo, R.L.2
  • 26
    • 72049089561 scopus 로고    scopus 로고
    • Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata
    • Ma, Y.F.; Liu, C.B.; Liu, X.H.; Wu, J.; Yang, H.L.; Wang, Y.P.; Li, J.X.; Yu, H.N.; Lai, R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. Genomics 2010, 95, 66-71.
    • (2010) Genomics , vol.95 , pp. 66-71
    • Ma, Y.F.1    Liu, C.B.2    Liu, X.H.3    Wu, J.4    Yang, H.L.5    Wang, Y.P.6    Li, J.X.7    Yu, H.N.8    Lai, R.9
  • 27
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark, D.; Steiner, H.; Rasmuson, T.; Boman, H.G. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur. J. Biochem. 1980, 106, 7-16.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 28
    • 0033043785 scopus 로고    scopus 로고
    • Mouse beta-defensin 3 is an inducible antimicrobial peptide expressed in the epithelia of multiple organs
    • Bals, R.; Wang, X.; Meegalla, R.L.; Wattler, S.; Weiner, D.J.; Nehls, M.C.; Wilson, J.M. Mouse beta-defensin 3 is an inducible antimicrobial peptide expressed in the epithelia of multiple organs. Infect. Immun. 1999, 67, 3542-3547.
    • (1999) Infect. Immun. , vol.67 , pp. 3542-3547
    • Bals, R.1    Wang, X.2    Meegalla, R.L.3    Wattler, S.4    Weiner, D.J.5    Nehls, M.C.6    Wilson, J.M.7
  • 29
    • 0042905861 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in innate immunity
    • Ganz, T. The role of antimicrobial peptides in innate immunity. Integr. Comp. Biol. 2003, 43, 300-304.
    • (2003) Integr. Comp. Biol. , vol.43 , pp. 300-304
    • Ganz, T.1
  • 30
    • 0036208192 scopus 로고    scopus 로고
    • Epithelial cell-derived human beta-defensin-2 acts as a chemotaxin for mast cells through a pertussis toxin-sensitive and phospholipase c-dependent pathway
    • Niyonsaba, F.; Iwabuchi, K.; Matsuda, H.; Ogawa, H.; Nagaoka, I. Epithelial cell-derived human beta-defensin-2 acts as a chemotaxin for mast cells through a pertussis toxin-sensitive and phospholipase c-dependent pathway. Int. Immunol. 2002, 14, 421-426.
    • (2002) Int. Immunol. , vol.14 , pp. 421-426
    • Niyonsaba, F.1    Iwabuchi, K.2    Matsuda, H.3    Ogawa, H.4    Nagaoka, I.5
  • 31
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock, R.E.; Scott, M.G. The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. USA 2000, 97, 8856-8861.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 32
    • 0142218765 scopus 로고    scopus 로고
    • Roles of antimicrobial peptides such as defensins in innate and adaptive immunity
    • Oppenheim, J.J.; Biragyn, A.; Kwak, L.W.; Yang, D. Roles of antimicrobial peptides such as defensins in innate and adaptive immunity. Ann. Rheum. Dis. 2003, 62, ii17-ii21.
    • (2003) Ann. Rheum. Dis. , vol.62
    • Oppenheim, J.J.1    Biragyn, A.2    Kwak, L.W.3    Yang, D.4
  • 33
    • 0034665513 scopus 로고    scopus 로고
    • An alpha-helical cationic antimicrobial peptide selectively modulates macrophage responses to lipopolysaccharide and directly alters macrophage gene expression
    • Scott, M.G.; Rosenberger, C.M.; Gold, M.R.; Finlay, B.B.; Hancock, R.E. An alpha-helical cationic antimicrobial peptide selectively modulates macrophage responses to lipopolysaccharide and directly alters macrophage gene expression. J. Immunol. 2000, 165, 3358-3365.
    • (2000) J. Immunol. , vol.165 , pp. 3358-3365
    • Scott, M.G.1    Rosenberger, C.M.2    Gold, M.R.3    Finlay, B.B.4    Hancock, R.E.5
  • 34
    • 84863331840 scopus 로고    scopus 로고
    • Signaling pathways mediating chemokine induction in keratinocytes by cathelicidin ll-37 and flagellin
    • Nijnik, A.; Pistolic, J.; Filewod, N.C.; Hancock, R.E. Signaling pathways mediating chemokine induction in keratinocytes by cathelicidin ll-37 and flagellin. J. Innate Immun. 2012, 4, 377-386.
    • (2012) J. Innate Immun. , vol.4 , pp. 377-386
    • Nijnik, A.1    Pistolic, J.2    Filewod, N.C.3    Hancock, R.E.4
  • 36
    • 0035190972 scopus 로고    scopus 로고
    • Human toll-like receptor 2 mediates induction of the antimicrobial peptide human beta-defensin 2 in response to bacterial lipoprotein
    • Birchler, T.; Seibl, R.; Buchner, K.; Loeliger, S.; Seger, R.; Hossle, J.P.; Aguzzi, A.; Lauener, R.P. Human toll-like receptor 2 mediates induction of the antimicrobial peptide human beta-defensin 2 in response to bacterial lipoprotein. Eur. J. Immunol. 2001, 31, 3131-3137.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 3131-3137
    • Birchler, T.1    Seibl, R.2    Buchner, K.3    Loeliger, S.4    Seger, R.5    Hossle, J.P.6    Aguzzi, A.7    Lauener, R.P.8
  • 38
    • 0030994620 scopus 로고    scopus 로고
    • A synthetic lipopolysaccharide-binding peptide based on the neutrophil-derived protein cap37 prevents endotoxin-induced responses in conscious rats
    • Brackett, D.J.; Lerner, M.R.; Lacquement, M.A.; He, R.; Pereira, H.A. A synthetic lipopolysaccharide-binding peptide based on the neutrophil-derived protein cap37 prevents endotoxin-induced responses in conscious rats. Infect. Immun. 1997, 65, 2803-2811.
    • (1997) Infect. Immun. , vol.65 , pp. 2803-2811
    • Brackett, D.J.1    Lerner, M.R.2    Lacquement, M.A.3    He, R.4    Pereira, H.A.5
  • 39
    • 0032975547 scopus 로고    scopus 로고
    • Neutralization of endotoxin in vitro and in vivo by a human lactoferrin-derived peptide
    • Zhang, G.H.; Mann, D.M.; Tsai, C.M. Neutralization of endotoxin in vitro and in vivo by a human lactoferrin-derived peptide. Infect. Immun. 1999, 67, 1353-1358.
    • (1999) Infect. Immun. , vol.67 , pp. 1353-1358
    • Zhang, G.H.1    Mann, D.M.2    Tsai, C.M.3
  • 40
    • 0025188131 scopus 로고
    • Cytokine induction by lipopolysaccharide (LPS) corresponds to lethal toxicity and is inhibited by nontoxic Rhodobacter capsulatus LPS
    • Loppnow, H.; Libby, P.; Freudenberg, M.; Krauss, J.H.; Weckesser, J.; Mayer, H. Cytokine induction by lipopolysaccharide (LPS) corresponds to lethal toxicity and is inhibited by nontoxic Rhodobacter capsulatus LPS. Infect. Immun. 1990, 58, 3743-3750.
    • (1990) Infect. Immun. , vol.58 , pp. 3743-3750
    • Loppnow, H.1    Libby, P.2    Freudenberg, M.3    Krauss, J.H.4    Weckesser, J.5    Mayer, H.6
  • 41
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers, J.P.; Hancock, R.E. The relationship between peptide structure and antibacterial activity. Peptides 2003, 24, 1681-1691.
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 42
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • Bulet, P.; Stocklin, R.; Menin, L. Anti-microbial peptides: From invertebrates to vertebrates. Immunol. Rev. 2004, 198, 169-184.
    • (2004) Immunol. Rev. , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 44
    • 0141817944 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin p and a sakacin p variant that is structurally stabilized by an inserted c-terminal disulfide bridge
    • Uteng, M.; Hauge, H.H.; Markwick, P.R.; Fimland, G.; Mantzilas, D.; Nissen-Meyer, J.; Muhle-Goll, C. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin p and a sakacin p variant that is structurally stabilized by an inserted c-terminal disulfide bridge. Biochemistry 2003, 42, 11417-11426.
    • (2003) Biochemistry , vol.42 , pp. 11417-11426
    • Uteng, M.1    Hauge, H.H.2    Markwick, P.R.3    Fimland, G.4    Mantzilas, D.5    Nissen-Meyer, J.6    Muhle-Goll, C.7
  • 45
    • 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
  • 46
    • 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
  • 48
    • 0035824437 scopus 로고    scopus 로고
    • Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase
    • Loeffler, J.M.; Nelson, D.; Fischetti, V.A. Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase. Science 2001, 294, 2170-2172.
    • (2001) Science , vol.294 , pp. 2170-2172
    • Loeffler, J.M.1    Nelson, D.2    Fischetti, V.A.3
  • 49
    • 84858003063 scopus 로고    scopus 로고
    • Antibiotic and antimicrobial peptide combinations: Synergistic inhibition of Pseudomonas fluorescens and antibiotic-resistant variants
    • Naghmouchi, K.; le Lay, C.; Baah, J.; Drider, D. Antibiotic and antimicrobial peptide combinations: Synergistic inhibition of Pseudomonas fluorescens and antibiotic-resistant variants. Res. Microbiol. 2012, 163, 101-108.
    • (2012) Res. Microbiol. , vol.163 , pp. 101-108
    • Naghmouchi, K.1    le Lay, C.2    Baah, J.3    Drider, D.4
  • 50
    • 79952187401 scopus 로고    scopus 로고
    • Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces
    • Costa, F.; Carvalho, I.F.; Montelaro, R.C.; Gomes, P.; Martins, M.C. Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces. Acta Biomater. 2011, 7, 1431-1440.
    • (2011) Acta Biomater. , vol.7 , pp. 1431-1440
    • Costa, F.1    Carvalho, I.F.2    Montelaro, R.C.3    Gomes, P.4    Martins, M.C.5
  • 51
    • 84872678746 scopus 로고    scopus 로고
    • Chemical synthesis and biological evaluation of an antimicrobial peptide gonococcal growth inhibitor
    • Wade, J.D.; Lin, F.; Hossain, M.A.; Dawson, R.M. Chemical synthesis and biological evaluation of an antimicrobial peptide gonococcal growth inhibitor. Amino Acids 2012, 43, 2279-2283.
    • (2012) Amino Acids , vol.43 , pp. 2279-2283
    • Wade, J.D.1    Lin, F.2    Hossain, M.A.3    Dawson, R.M.4
  • 52
    • 0027445909 scopus 로고
    • Recombinant DNA procedures for producing small antimicrobial cationic peptides in bacteria
    • Piers, K.L.; Brown, M.H.; Hancock, R.E. Recombinant DNA procedures for producing small antimicrobial cationic peptides in bacteria. Gene 1993, 134, 7-13.
    • (1993) Gene , vol.134 , pp. 7-13
    • Piers, K.L.1    Brown, M.H.2    Hancock, R.E.3
  • 53
    • 84873301395 scopus 로고    scopus 로고
    • Recombinant expression and purification of the antimicrobial peptide magainin-2
    • Ramos, R.; Moreira, S.; Rodrigues, A.; Gama, M.; Domingues, L. Recombinant expression and purification of the antimicrobial peptide magainin-2. Biotechnol. Prog. 2013, 29, 17-22.
    • (2013) Biotechnol. Prog. , vol.29 , pp. 17-22
    • Ramos, R.1    Moreira, S.2    Rodrigues, A.3    Gama, M.4    Domingues, L.5
  • 54
    • 0037072808 scopus 로고    scopus 로고
    • The consequence of sequence alteration of an amphipathic alpha-helical antimicrobial peptide and its diastereomers
    • Papo, N.; Oren, Z.; Pag, U.; Sahl, H.G.; Shai, Y. The consequence of sequence alteration of an amphipathic alpha-helical antimicrobial peptide and its diastereomers. J. Biol. Chem. 2002, 277, 33913-33921.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33913-33921
    • Papo, N.1    Oren, Z.2    Pag, U.3    Sahl, H.G.4    Shai, Y.5
  • 55
    • 0036736465 scopus 로고    scopus 로고
    • Analysis of the cytotoxicity of synthetic antimicrobial peptides on mouse leucocytes: Implications for systemic use
    • Pacor, S.; Giangaspero, A.; Bacac, M.; Sava, G.; Tossi, A. Analysis of the cytotoxicity of synthetic antimicrobial peptides on mouse leucocytes: Implications for systemic use. J. Antimicrob. Chemother. 2002, 50, 339-348.
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 339-348
    • Pacor, S.1    Giangaspero, A.2    Bacac, M.3    Sava, G.4    Tossi, A.5
  • 56
    • 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
  • 59
    • 33645767676 scopus 로고    scopus 로고
    • Adding selectivity to antimicrobial peptides: Rational design of a multidomain peptide against Pseudomonas spp
    • Eckert, R.; Qi, F.; Yarbrough, D.K.; He, J.; Anderson, M.H.; Shi, W. Adding selectivity to antimicrobial peptides: Rational design of a multidomain peptide against Pseudomonas spp. Antimicrob. Agents Chemother. 2006, 50, 1480-1488.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1480-1488
    • Eckert, R.1    Qi, F.2    Yarbrough, D.K.3    He, J.4    Anderson, M.H.5    Shi, W.6
  • 62
    • 62949184998 scopus 로고    scopus 로고
    • Immobilization reduces the activity of surface-bound cationic antimicrobial peptides with no influence upon the activity spectrum
    • Bagheri, M.; Beyermann, M.; Dathe, M. Immobilization reduces the activity of surface-bound cationic antimicrobial peptides with no influence upon the activity spectrum. Antimicrob. Agents Chemother. 2009, 53, 1132-1141.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1132-1141
    • Bagheri, M.1    Beyermann, M.2    Dathe, M.3
  • 64
    • 33748413776 scopus 로고    scopus 로고
    • Antibacterial peptides for therapeutic use: Obstacles and realistic outlook
    • Marr, A.K.; Gooderham, W.J.; Hancock, R.E. Antibacterial peptides for therapeutic use: Obstacles and realistic outlook. Curr. Opin. Pharmacol. 2006, 6, 468-472.
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 468-472
    • Marr, A.K.1    Gooderham, W.J.2    Hancock, R.E.3
  • 66
    • 0034869858 scopus 로고    scopus 로고
    • The lysozyme mechanism sorted-After 50 years
    • Kirby, A.J. The lysozyme mechanism sorted-After 50 years. Nat. Struct. Biol. 2001, 8, 737-739.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 737-739
    • Kirby, A.J.1
  • 67
    • 0035885441 scopus 로고    scopus 로고
    • Human alpha-defensin 1 (hnp-1) inhibits adenoviral infection in vitro
    • Bastian, A.; Schafer, H. Human alpha-defensin 1 (hnp-1) inhibits adenoviral infection in vitro. Regul. Pept. 2001, 101, 157-161.
    • (2001) Regul. Pept. , vol.101 , pp. 157-161
    • Bastian, A.1    Schafer, H.2
  • 69
    • 0031940688 scopus 로고    scopus 로고
    • Anti-hiv-1 activity of indolicidin, an antimicrobial peptide from neutrophils
    • Robinson, W.E., Jr.; McDougall, B.; Tran, D.; Selsted, M.E. Anti-hiv-1 activity of indolicidin, an antimicrobial peptide from neutrophils. J. Leukoc. Biol. 1998, 63, 94-100.
    • (1998) J. Leukoc. Biol. , vol.63 , pp. 94-100
    • Robinson Jr., W.E.1    McDougall, B.2    Tran, D.3    Selsted, M.E.4
  • 70
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity
    • Sitaram, N.; Nagaraj, R. Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity. Biochim. Biophys. Acta 1999, 1462, 29-54.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 71
    • 0036137074 scopus 로고    scopus 로고
    • In vitro antiviral activity of dermaseptins against herpes simplex virus type 1
    • Belaid, A.; Aouni, M.; Khelifa, R.; Trabelsi, A.; Jemmali, M.; Hani, K. In vitro antiviral activity of dermaseptins against herpes simplex virus type 1. J. Med. Virol. 2002, 66, 229-234.
    • (2002) J. Med. Virol. , vol.66 , pp. 229-234
    • Belaid, A.1    Aouni, M.2    Khelifa, R.3    Trabelsi, A.4    Jemmali, M.5    Hani, K.6
  • 72
    • 2342573669 scopus 로고    scopus 로고
    • Theta defensins protect cells from infection by herpes simplex virus by inhibiting viral adhesion and entry
    • Yasin, B.; Wang, W.; Pang, M.; Cheshenko, N.; Hong, T.; Waring, A.J.; Herold, B.C.; Wagar, E.A.; Lehrer, R.I. Theta defensins protect cells from infection by herpes simplex virus by inhibiting viral adhesion and entry. J. Virol. 2004, 78, 5147-5156.
    • (2004) J. Virol. , vol.78 , pp. 5147-5156
    • Yasin, B.1    Wang, W.2    Pang, M.3    Cheshenko, N.4    Hong, T.5    Waring, A.J.6    Herold, B.C.7    Wagar, E.A.8    Lehrer, R.I.9
  • 73
    • 0030583701 scopus 로고    scopus 로고
    • Analysis of the interaction of an anti-hiv peptide, t22 ([tyr5, 12, lys7]-polyphemusin ii), with gp120 and cd4 by surface plasmon resonance
    • Tamamura, H.; Ishihara, T.; Otaka, A.; Murakami, T.; Ibuka, T.; Waki, M.; Matsumoto, A.; Yamamoto, N.; Fujii, N. Analysis of the interaction of an anti-hiv peptide, t22 ([tyr5, 12, lys7]-polyphemusin ii), with gp120 and cd4 by surface plasmon resonance. Biochim. Biophys. Acta 1996, 1298, 37-44.
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 37-44
    • Tamamura, H.1    Ishihara, T.2    Otaka, A.3    Murakami, T.4    Ibuka, T.5    Waki, M.6    Matsumoto, A.7    Yamamoto, N.8    Fujii, N.9
  • 74
    • 0034795499 scopus 로고    scopus 로고
    • Human cytomegalovirus binding to heparan sulfate proteoglycans on the cell surface and/or entry stimulates the expression of human leukocyte antigen class I
    • Song, B.H.; Lee, G.C.; Moon, M.S.; Cho, Y.H.; Lee, C.H. Human cytomegalovirus binding to heparan sulfate proteoglycans on the cell surface and/or entry stimulates the expression of human leukocyte antigen class I. J. Gen. Virol. 2001, 82, 2405-2413.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2405-2413
    • Song, B.H.1    Lee, G.C.2    Moon, M.S.3    Cho, Y.H.4    Lee, C.H.5
  • 75
    • 0024497174 scopus 로고
    • Initial interaction of herpes simplex virus with cells is binding to heparan sulfate
    • WuDunn, D.; Spear, P.G. Initial interaction of herpes simplex virus with cells is binding to heparan sulfate. J. Virol. 1989, 63, 52-58.
    • (1989) J. Virol. , vol.63 , pp. 52-58
    • WuDunn, D.1    Spear, P.G.2
  • 76
    • 0031746910 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan binding by herpes simplex virus type 1 glycoproteins b and c, which differ in their contributions to virus attachment, penetration, and cell-to-cell spread
    • Laquerre, S.; Argnani, R.; Anderson, D.B.; Zucchini, S.; Manservigi, R.; Glorioso, J.C. Heparan sulfate proteoglycan binding by herpes simplex virus type 1 glycoproteins b and c, which differ in their contributions to virus attachment, penetration, and cell-to-cell spread. J. Virol. 1998, 72, 6119-6130.
    • (1998) J. Virol. , vol.72 , pp. 6119-6130
    • Laquerre, S.1    Argnani, R.2    Anderson, D.B.3    Zucchini, S.4    Manservigi, R.5    Glorioso, J.C.6
  • 77
    • 4344615913 scopus 로고    scopus 로고
    • Anti-hsv activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface
    • Andersen, J.H.; Jenssen, H.; Sandvik, K.; Gutteberg, T.J. Anti-hsv activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface. J. Med. Virol. 2004, 74, 262-271.
    • (2004) J. Med. Virol. , vol.74 , pp. 262-271
    • Andersen, J.H.1    Jenssen, H.2    Sandvik, K.3    Gutteberg, T.J.4
  • 78
    • 0344304749 scopus 로고    scopus 로고
    • Anti-hsv activity of lactoferricin analogues is only partly related to their affinity for heparan sulfate
    • Jenssen, H.; Andersen, J.H.; Uhlin-Hansen, L.; Gutteberg, T.J.; Rekdal, O. Anti-hsv activity of lactoferricin analogues is only partly related to their affinity for heparan sulfate. Antiviral Res. 2004, 61, 101-109.
    • (2004) Antiviral Res. , vol.61 , pp. 101-109
    • Jenssen, H.1    Andersen, J.H.2    Uhlin-Hansen, L.3    Gutteberg, T.J.4    Rekdal, O.5
  • 79
    • 0033166256 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein vp16
    • Liu, Y.; Gong, W.; Huang, C.C.; Herr, W.; Cheng, X. Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein vp16. Genes Dev. 1999, 13, 1692-1703.
    • (1999) Genes Dev. , vol.13 , pp. 1692-1703
    • Liu, Y.1    Gong, W.2    Huang, C.C.3    Herr, W.4    Cheng, X.5
  • 80
    • 0037308626 scopus 로고    scopus 로고
    • Np-1, a rabbit alpha-defensin, prevents the entry and intercellular spread of herpes simplex virus type 2
    • Sinha, S.; Cheshenko, N.; Lehrer, R.I.; Herold, B.C. Np-1, a rabbit alpha-defensin, prevents the entry and intercellular spread of herpes simplex virus type 2. Antimicrob. Agents Chemother. 2003, 47, 494-500.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 494-500
    • Sinha, S.1    Cheshenko, N.2    Lehrer, R.I.3    Herold, B.C.4
  • 81
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 2002, 66, 236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 82
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • Zhang, L.; Rozek, A.; Hancock, R.E. Interaction of cationic antimicrobial peptides with model membranes. J. Biol. Chem. 2001, 276, 35714-35722.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35714-35722
    • Zhang, L.1    Rozek, A.2    Hancock, R.E.3
  • 83
    • 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
  • 84
    • 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
  • 86
    • 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. 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
  • 87
    • 0036848132 scopus 로고    scopus 로고
    • Nisin, alone and combined with peptidoglycan-modulating antibiotics: Activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci
    • Brumfitt, W.; Salton, M.R.; Hamilton-Miller, J.M. Nisin, alone and combined with peptidoglycan-modulating antibiotics: Activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci. J. Antimicrob. Chemother. 2002, 50, 731-734.
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 731-734
    • Brumfitt, W.1    Salton, M.R.2    Hamilton-Miller, J.M.3
  • 88
    • 0031646792 scopus 로고    scopus 로고
    • Fungicidal and binding properties of the natural peptides cecropin b and dermaseptin
    • De Lucca, A.J.; Bland, J.M.; Jacks, T.J.; Grimm, C.; Walsh, T.J. Fungicidal and binding properties of the natural peptides cecropin b and dermaseptin. Med. Mycol. 1998, 36, 291-298.
    • (1998) Med. Mycol. , vol.36 , pp. 291-298
    • De Lucca, A.J.1    Bland, J.M.2    Jacks, T.J.3    Grimm, C.4    Walsh, T.J.5
  • 89
    • 0032958766 scopus 로고    scopus 로고
    • Antifungal peptides: Novel therapeutic compounds against emerging pathogens
    • De Lucca, A.J.; Walsh, T.J. Antifungal peptides: Novel therapeutic compounds against emerging pathogens. Antimicrob. Agents Chemother. 1999, 43, 1-11.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1-11
    • De Lucca, A.J.1    Walsh, T.J.2
  • 91
    • 67849130752 scopus 로고    scopus 로고
    • The chitin-binding capability of cy-amp1 from cycad is essential to antifungal activity
    • Yokoyama, S.; Iida, Y.; Kawasaki, Y.; Minami, Y.; Watanabe, K.; Yagi, F. The chitin-binding capability of cy-amp1 from cycad is essential to antifungal activity. J. Pept. Sci. 2009, 15, 492-497.
    • (2009) J. Pept. Sci. , vol.15 , pp. 492-497
    • Yokoyama, S.1    Iida, Y.2    Kawasaki, Y.3    Minami, Y.4    Watanabe, K.5    Yagi, F.6
  • 93
    • 4544223087 scopus 로고    scopus 로고
    • Purification, characterization, and sequencing of novel antimicrobial peptides, Tu-AMP 1 and Tu-AMP 2, from bulbs of tulip (Tulipa gesneriana L.)
    • Fujimura, M.; Ideguchi, M.; Minami, Y.; Watanabe, K.; Tadera, K. Purification, characterization, and sequencing of novel antimicrobial peptides, Tu-AMP 1 and Tu-AMP 2, from bulbs of tulip (Tulipa gesneriana L.). Biosci. Biotechnol. Biochem. 2004, 68, 571-577.
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 571-577
    • Fujimura, M.1    Ideguchi, M.2    Minami, Y.3    Watanabe, K.4    Tadera, K.5
  • 94
    • 0021847049 scopus 로고
    • Correlation of binding of rabbit granulocyte peptides to Candida albicans with candidacidal activity
    • Lehrer, R.I.; Szklarek, D.; Ganz, T.; Selsted, M.E. Correlation of binding of rabbit granulocyte peptides to Candida albicans with candidacidal activity. Infect. Immun. 1985, 49, 207-211.
    • (1985) Infect. Immun. , vol.49 , pp. 207-211
    • Lehrer, R.I.1    Szklarek, D.2    Ganz, T.3    Selsted, M.E.4
  • 96
    • 78549295936 scopus 로고    scopus 로고
    • Permeabilization of fungal hyphae by the plant defensin nad1 occurs through a cell wall-dependent process
    • Van der Weerden, N.L.; Hancock, R.E.; Anderson, M.A. Permeabilization of fungal hyphae by the plant defensin nad1 occurs through a cell wall-dependent process. J. Biol. Chem. 2010, 285, 37513-37520.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37513-37520
    • Van der Weerden, N.L.1    Hancock, R.E.2    Anderson, M.A.3
  • 98
    • 46749108538 scopus 로고    scopus 로고
    • Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alpha-helical cationic antimicrobial peptides
    • Jiang, Z.; Vasil, A.I.; Hale, J.D.; Hancock, R.E.; Vasil, M.L.; Hodges, R.S. Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alpha-helical cationic antimicrobial peptides. Biopolymers 2008, 90, 369-383.
    • (2008) Biopolymers , vol.90 , pp. 369-383
    • Jiang, Z.1    Vasil, A.I.2    Hale, J.D.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 99
    • 1442338547 scopus 로고    scopus 로고
    • Structure and fungicidal activity of a synthetic antimicrobial peptide, p18, and its truncated peptides
    • Lee, D.G.; Hahm, K.S.; Shin, S.Y. Structure and fungicidal activity of a synthetic antimicrobial peptide, p18, and its truncated peptides. Biotechnol. Lett. 2004, 26, 337-341.
    • (2004) Biotechnol. Lett. , vol.26 , pp. 337-341
    • Lee, D.G.1    Hahm, K.S.2    Shin, S.Y.3
  • 101
    • 0346850585 scopus 로고    scopus 로고
    • Solution structure of alo-3: A new knottin-type antifungal peptide from the insect Acrocinus longimanus
    • Barbault, F.; Landon, C.; Guenneugues, M.; Meyer, J.P.; Schott, V.; Dimarcq, J.L.; Vovelle, F. Solution structure of alo-3: A new knottin-type antifungal peptide from the insect Acrocinus longimanus. Biochemistry 2003, 42, 14434-14442.
    • (2003) Biochemistry , vol.42 , pp. 14434-14442
    • Barbault, F.1    Landon, C.2    Guenneugues, M.3    Meyer, J.P.4    Schott, V.5    Dimarcq, J.L.6    Vovelle, F.7
  • 102
    • 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
  • 104
    • 2342603487 scopus 로고    scopus 로고
    • Antinematodal effect of antimicrobial peptide, pmap-23, isolated from porcine myeloid against Caenorhabditis elegans
    • Park, Y.; Jang, S.H.; Lee, D.G.; Hahm, K.S. Antinematodal effect of antimicrobial peptide, pmap-23, isolated from porcine myeloid against Caenorhabditis elegans. J. Pept. Sci. 2004, 10, 304-311.
    • (2004) J. Pept. Sci. , vol.10 , pp. 304-311
    • Park, Y.1    Jang, S.H.2    Lee, D.G.3    Hahm, K.S.4
  • 105
    • 0030845025 scopus 로고    scopus 로고
    • Small, anionic, and charge-neutralizing propeptide fragments of zymogens are antimicrobial
    • Brogden, K.A.; Ackermann, M.; Huttner, K.M. Small, anionic, and charge-neutralizing propeptide fragments of zymogens are antimicrobial. Antimicrob. Agents Chemother. 1997, 41, 1615-1617.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1615-1617
    • Brogden, K.A.1    Ackermann, M.2    Huttner, K.M.3
  • 106
    • 0036375765 scopus 로고    scopus 로고
    • An anionic antimicrobial peptide from toad Bombina maxima
    • Lai, R.; Liu, H.; Lee, W.H.; Zhang, Y. An anionic antimicrobial peptide from toad Bombina maxima. Biochem. Bioph. Res. Co. 2002, 295, 796-799.
    • (2002) Biochem. Bioph. Res. Co. , vol.295 , pp. 796-799
    • Lai, R.1    Liu, H.2    Lee, W.H.3    Zhang, Y.4
  • 109
    • 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
  • 110
    • 5144233793 scopus 로고    scopus 로고
    • Synthesis and hiv-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin
    • Krajewski, K.; Marchand, C.; Long, Y.Q.; Pommier, Y.; Roller, P.P. Synthesis and hiv-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. Bioorg. Med. Chem. Lett. 2004, 14, 5595-5598.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 5595-5598
    • Krajewski, K.1    Marchand, C.2    Long, Y.Q.3    Pommier, Y.4    Roller, P.P.5
  • 111
    • 0036293431 scopus 로고    scopus 로고
    • Design of novel peptide analogs with potent fungicidal activity, based on pmap-23 antimicrobial peptide isolated from porcine myeloid
    • Lee, D.G.; Kim, P.I.; Park, Y.K.; Woo, E.R.; Choi, J.S.; Choi, C.H.; Hahm, K.S. Design of novel peptide analogs with potent fungicidal activity, based on pmap-23 antimicrobial peptide isolated from porcine myeloid. Biochem. Bioph. Res. Co. 2002, 293, 231-238.
    • (2002) Biochem. Bioph. Res. Co. , vol.293 , pp. 231-238
    • Lee, D.G.1    Kim, P.I.2    Park, Y.K.3    Woo, E.R.4    Choi, J.S.5    Choi, C.H.6    Hahm, K.S.7
  • 112
    • 66349100178 scopus 로고    scopus 로고
    • Transcriptional regulation in bacterial membrane lipid synthesis
    • Zhang, Y.M.; Rock, C.O. Transcriptional regulation in bacterial membrane lipid synthesis. J. Lipid Res. 2009, 50, S115-S119.
    • (2009) J. Lipid Res. , vol.50
    • Zhang, Y.M.1    Rock, C.O.2
  • 113
    • 0030028241 scopus 로고    scopus 로고
    • Neutron scattering in the plane of membranes: Structure of alamethicin pores
    • He, K.; Ludtke, S.J.; Worcester, D.L.; Huang, H.W. Neutron scattering in the plane of membranes: Structure of alamethicin pores. Biophys. J. 1996, 70, 2659-2666.
    • (1996) Biophys. J. , vol.70 , pp. 2659-2666
    • He, K.1    Ludtke, S.J.2    Worcester, D.L.3    Huang, H.W.4
  • 114
    • 79959365312 scopus 로고    scopus 로고
    • Mechanisms of cellular uptake of cell-penetrating peptides
    • Madani, F.; Lindberg, S.; Langel, U.; Futaki, S.; Graslund, A. Mechanisms of cellular uptake of cell-penetrating peptides. J. Biophys. 2011, 2011, 414729.
    • (2011) J. Biophys. , vol.2011 , pp. 414729
    • Madani, F.1    Lindberg, S.2    Langel, U.3    Futaki, S.4    Graslund, A.5
  • 115
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny, Y.; Rapaport, D.; Mor, A.; Nicolas, P.; Shai, Y. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 1992, 31, 12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 116
    • 20444400818 scopus 로고    scopus 로고
    • Detergent-like properties of magainin antibiotic peptides: A 31p solid-state nmr spectroscopy study
    • Bechinger, B. Detergent-like properties of magainin antibiotic peptides: A 31p solid-state nmr spectroscopy study. Biochim. Biophys. Acta 2005, 1712, 101-108.
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 101-108
    • Bechinger, B.1
  • 117
    • 78650521954 scopus 로고    scopus 로고
    • Computational studies of protegrin antimicrobial peptides: A review
    • Bolintineanu, D.S.; Kaznessis, Y.N. Computational studies of protegrin antimicrobial peptides: A review. Peptides 2011, 32, 188-201.
    • (2011) Peptides , vol.32 , pp. 188-201
    • Bolintineanu, D.S.1    Kaznessis, Y.N.2
  • 118
    • 28444457793 scopus 로고    scopus 로고
    • Membrane thinning due to antimicrobial peptide binding: An atomic force microscopy study of msi-78 in lipid bilayers
    • Mecke, A.; Lee, D.K.; Ramamoorthy, A.; Orr, B.G.; Holl, M.M.B. Membrane thinning due to antimicrobial peptide binding: An atomic force microscopy study of msi-78 in lipid bilayers. Biophys. J. 2005, 89, 4043-4050.
    • (2005) Biophys. J. , vol.89 , pp. 4043-4050
    • Mecke, A.1    Lee, D.K.2    Ramamoorthy, A.3    Orr, B.G.4    Holl, M.M.B.5
  • 119
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • Ludtke, S.; He, K.; Huang, H. Membrane thinning caused by magainin 2. Biochemistry 1995, 34, 16764-16769.
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.1    He, K.2    Huang, H.3
  • 120
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • Chen, F.Y.; Lee, M.T.; Huang, H.W. Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophys. J. 2003, 84, 3751-3758.
    • (2003) Biophys. J. , vol.84 , pp. 3751-3758
    • Chen, F.Y.1    Lee, M.T.2    Huang, H.W.3
  • 121
    • 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
  • 122
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • Matsuzaki, K. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta Biomembr. 1998, 1376, 391-400.
    • (1998) Biochim. Biophys. Acta Biomembr. , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 123
    • 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
  • 124
    • 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
  • 126
    • 0036214967 scopus 로고    scopus 로고
    • Intracellular targets of antibacterial peptides
    • Cudic, M.; Otvos, L. Intracellular targets of antibacterial peptides. Curr. Drug Targets 2002, 3, 101-106.
    • (2002) Curr. Drug Targets , vol.3 , pp. 101-106
    • Cudic, M.1    Otvos, L.2
  • 127
    • 28044443162 scopus 로고    scopus 로고
    • Antibacterial peptides and proteins with multiple cellular targets
    • Otvos, L. Antibacterial peptides and proteins with multiple cellular targets. J. Pept. Sci. 2005, 11, 697-706.
    • (2005) J. Pept. Sci. , vol.11 , pp. 697-706
    • Otvos, L.1
  • 129
    • 34548145634 scopus 로고    scopus 로고
    • Cell-penetrating peptides in drug development: Enabling intracellular targets
    • Chen, L.; Harrison, S.D. Cell-penetrating peptides in drug development: Enabling intracellular targets. Biochem. Soc. Trans. 2007, 35, 821-825.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 821-825
    • Chen, L.1    Harrison, S.D.2
  • 131
    • 70350435548 scopus 로고    scopus 로고
    • Multifunctional host defense peptides: Intracellular-targeting antimicrobial peptides
    • Nicolas, P. Multifunctional host defense peptides: Intracellular-targeting antimicrobial peptides. FEBS J. 2009, 276, 6483-6496.
    • (2009) FEBS J. , vol.276 , pp. 6483-6496
    • Nicolas, P.1
  • 133
    • 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
  • 134
    • 0032952408 scopus 로고    scopus 로고
    • In vitro antibacterial activities of platelet microbicidal protein and neutrophil defensin against Staphylococcus aureus are influenced by antibiotics differing in mechanism of action
    • Xiong, Y.Q.; Yeaman, M.R.; Bayer, A.S. In vitro antibacterial activities of platelet microbicidal protein and neutrophil defensin against Staphylococcus aureus are influenced by antibiotics differing in mechanism of action. Antimicrob. Agents Chemother. 1999, 43, 1111-1117.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1111-1117
    • Xiong, Y.Q.1    Yeaman, M.R.2    Bayer, A.S.3
  • 135
    • 0032748297 scopus 로고    scopus 로고
    • Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets
    • Castle, M.; Nazarian, A.; Yi, S.S.; Tempst, P. Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets. J. Biol. Chem. 1999, 274, 32555-32564.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32555-32564
    • Castle, M.1    Nazarian, A.2    Yi, S.S.3    Tempst, P.4
  • 136
    • 0025962890 scopus 로고
    • Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis
    • Nishikata, M.; Kanehira, T.; Oh, H.; Tani, H.; Tazaki, M.; Kuboki, Y. Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis. Biochem. Bioph. Res. Co. 1991, 174, 625-630.
    • (1991) Biochem. Bioph. Res. Co. , vol.174 , pp. 625-630
    • Nishikata, M.1    Kanehira, T.2    Oh, H.3    Tani, H.4    Tazaki, M.5    Kuboki, Y.6
  • 137
    • 0027318984 scopus 로고
    • Selective inhibition of microbial serine proteases by enap-2, an antimicrobial peptide from equine neutrophils
    • Couto, M.A.; Harwig, S.S.; Lehrer, R.I. Selective inhibition of microbial serine proteases by enap-2, an antimicrobial peptide from equine neutrophils. Infect. Immun. 1993, 61, 2991-2994.
    • (1993) Infect. Immun. , vol.61 , pp. 2991-2994
    • Couto, M.A.1    Harwig, S.S.2    Lehrer, R.I.3
  • 139
    • 0026706736 scopus 로고
    • Purification and characterization of a diptericin homologue from Sarcophaga peregrina (flesh fly)
    • Ishikawa, M.; Kubo, T.; Natori, S. Purification and characterization of a diptericin homologue from Sarcophaga peregrina (flesh fly). Biochem. J. 1992, 287, 573-578.
    • (1992) Biochem. J. , vol.287 , pp. 573-578
    • Ishikawa, M.1    Kubo, T.2    Natori, S.3
  • 140
    • 0018333860 scopus 로고
    • Seminaplasmin is a potent inhibitor of E. coli RNA polymerase in vivo
    • Scheit, K.H.; Reddy, E.S.; Bhargava, P.M. Seminaplasmin is a potent inhibitor of E. coli RNA polymerase in vivo. Nature 1979, 279, 728-731.
    • (1979) Nature , vol.279 , pp. 728-731
    • Scheit, K.H.1    Reddy, E.S.2    Bhargava, P.M.3
  • 141
    • 0025272516 scopus 로고
    • Isolation and characterization of autolysis-defective mutants of Escherichia coli that are resistant to the lytic activity of seminalplasmin
    • Chitnis, S.N.; Prasad, K.S.; Bhargava, P.M. Isolation and characterization of autolysis-defective mutants of Escherichia coli that are resistant to the lytic activity of seminalplasmin. J. Gen. Microbiol. 1990, 136, 463-469.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 463-469
    • Chitnis, S.N.1    Prasad, K.S.2    Bhargava, P.M.3
  • 143
    • 34548172649 scopus 로고    scopus 로고
    • Macropinocytosis: Searching for an endocytic identity and role in the uptake of cell penetrating peptides
    • Jones, A.T. Macropinocytosis: Searching for an endocytic identity and role in the uptake of cell penetrating peptides. J. Cell Mol. Med. 2007, 11, 670-684.
    • (2007) J. Cell Mol. Med. , vol.11 , pp. 670-684
    • Jones, A.T.1
  • 144
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • Mayor, S.; Pagano, R.E. Pathways of clathrin-independent endocytosis. Nat. Rev. Mol. Cell Biol. 2007, 8, 603-612.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 145
    • 0034713613 scopus 로고    scopus 로고
    • Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: Proline as a translocation promoting factor
    • Kobayashi, S.; Takeshima, K.; Park, C.B.; Kim, S.C.; Matsuzaki, K. Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: Proline as a translocation promoting factor. Biochemistry 2000, 39, 8648-8654.
    • (2000) Biochemistry , vol.39 , pp. 8648-8654
    • Kobayashi, S.1    Takeshima, K.2    Park, C.B.3    Kim, S.C.4    Matsuzaki, K.5
  • 146
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin ii, a histone h2a-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin ii
    • Park, C.B.; Yi, K.S.; Matsuzaki, K.; Kim, M.S.; Kim, S.C. Structure-activity analysis of buforin ii, a histone h2a-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin ii. Proc. Natl. Acad. Sci. USA 2000, 97, 8245-8250.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 147
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • Tossi, A.; Sandri, L.; Giangaspero, A. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 2000, 55, 4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 149
    • 0033057716 scopus 로고    scopus 로고
    • Biological activities of c-terminal 15-residue synthetic fragment of melittin: Design of an analog with improved antibacterial activity
    • Subbalakshmi, C.; Nagaraj, R.; Sitaram, N. Biological activities of c-terminal 15-residue synthetic fragment of melittin: Design of an analog with improved antibacterial activity. FEBS Lett. 1999, 448, 62-66.
    • (1999) FEBS Lett. , vol.448 , pp. 62-66
    • Subbalakshmi, C.1    Nagaraj, R.2    Sitaram, N.3
  • 150
    • 34247497750 scopus 로고    scopus 로고
    • Structure-activity relationship of hp (2-20) analog peptide: Enhanced antimicrobial activity by n-terminal random coil region deletion
    • Park, Y.; Park, S.C.; Park, H.K.; Shin, S.Y.; Kim, Y.; Hahm, K.S. Structure-activity relationship of hp (2-20) analog peptide: Enhanced antimicrobial activity by n-terminal random coil region deletion. Biopolymers 2007, 88, 199-207.
    • (2007) Biopolymers , vol.88 , pp. 199-207
    • Park, Y.1    Park, S.C.2    Park, H.K.3    Shin, S.Y.4    Kim, Y.5    Hahm, K.S.6
  • 151
    • 0029947232 scopus 로고    scopus 로고
    • A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from moses sole fish Pardachirus marmoratus
    • Oren, Z.; Shai, Y. A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from moses sole fish Pardachirus marmoratus. Eur. J. Biochem. 1996, 237, 303-310.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 303-310
    • Oren, Z.1    Shai, Y.2
  • 152
    • 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
  • 153
    • 0037194346 scopus 로고    scopus 로고
    • Design of novel analogue peptides with potent antibiotic activity based on the antimicrobial peptide, hp (2-20), derived from n-terminus of Helicobacter pylori ribosomal protein L1
    • Lee, D.G.; Kim, H.N.; Park, Y.K.; Kim, H.K.; Choi, B.H.; Choi, C.H.; Hahm, K.S. Design of novel analogue peptides with potent antibiotic activity based on the antimicrobial peptide, hp (2-20), derived from n-terminus of Helicobacter pylori ribosomal protein L1. Biochim. Biophys. Acta 2002, 1598, 185-194.
    • (2002) Biochim. Biophys. Acta , vol.1598 , pp. 185-194
    • Lee, D.G.1    Kim, H.N.2    Park, Y.K.3    Kim, H.K.4    Choi, B.H.5    Choi, C.H.6    Hahm, K.S.7
  • 154
    • 0037053317 scopus 로고    scopus 로고
    • Structural requirements for potent versus selective cytotoxicity for antimicrobial dermaseptin s4 derivatives
    • Kustanovich, I.; Shalev, D.E.; Mikhlin, M.; Gaidukov, L.; Mor, A. Structural requirements for potent versus selective cytotoxicity for antimicrobial dermaseptin s4 derivatives. J. Biol. Chem. 2002, 277, 16941-16951.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16941-16951
    • Kustanovich, I.1    Shalev, D.E.2    Mikhlin, M.3    Gaidukov, L.4    Mor, A.5
  • 155
    • 23944500330 scopus 로고    scopus 로고
    • Controlled alteration of the shape and conformational stability of alpha-helical cell-lytic peptides: Effect on mode of action and cell specificity
    • Zelezetsky, I.; Pacor, S.; Pag, U.; Papo, N.; Shai, Y.; Sahl, H.G.; Tossi, A. Controlled alteration of the shape and conformational stability of alpha-helical cell-lytic peptides: Effect on mode of action and cell specificity. Biochem. J. 2005, 390, 177-188.
    • (2005) Biochem. J. , vol.390 , pp. 177-188
    • Zelezetsky, I.1    Pacor, S.2    Pag, U.3    Papo, N.4    Shai, Y.5    Sahl, H.G.6    Tossi, A.7
  • 156
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides
    • Dathe, M.; Wieprecht, T.; Nikolenko, H.; Handel, L.; Maloy, W.L.; MacDonald, D.L.; Beyermann, M.; Bienert, M. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett. 1997, 403, 208-212.
    • (1997) FEBS Lett. , vol.403 , pp. 208-212
    • Dathe, M.1    Wieprecht, T.2    Nikolenko, H.3    Handel, L.4    Maloy, W.L.5    McDonald, D.L.6    Beyermann, M.7    Bienert, M.8
  • 157
    • 34250195381 scopus 로고    scopus 로고
    • Folding amphipathic helices into membranes: Amphiphilicity trumps hydrophobicity
    • Fernandez-Vidal, 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-Vidal, M.1    Jayasinghe, S.2    Ladokhin, A.S.3    White, S.H.4
  • 158
    • 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
  • 159
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic alpha helical antimicrobial peptides
    • Giangaspero, A.; Sandri, L.; Tossi, A. Amphipathic alpha helical antimicrobial peptides. Eur. J. Biochem. 2001, 268, 5589-5600.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 162
    • 0030048407 scopus 로고    scopus 로고
    • The c-terminal bisphosphorylated proenkephalin-a-(209-237)-peptide from adrenal medullary chromaffin granules possesses antibacterial activity
    • Goumon, Y.; Strub, J.M.; Moniatte, M.; Nullans, G.; Poteur, L.; Hubert, P.; van Dorsselaer, A.; Aunis, D.; Metz-Boutigue, M.H. The c-terminal bisphosphorylated proenkephalin-a-(209-237)-peptide from adrenal medullary chromaffin granules possesses antibacterial activity. Eur. J. Biochem. 1996, 235, 516-525.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 516-525
    • Goumon, Y.1    Strub, J.M.2    Moniatte, M.3    Nullans, G.4    Poteur, L.5    Hubert, P.6    van Dorsselaer, A.7    Aunis, D.8    Metz-Boutigue, M.H.9
  • 163
    • 0031006967 scopus 로고    scopus 로고
    • D-amino acids in animal peptides
    • Kreil, G. D-amino acids in animal peptides. Annu. Rev. Biochem. 1997, 66, 337-345.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 337-345
    • Kreil, G.1
  • 164
    • 0026083012 scopus 로고
    • Isolation of achatin-I, a neuroactive tetrapeptide having a D-phenylalanine residue, from Achatina ganglia, and its effects on Achatina giant neurones
    • Kamatani, Y.; Minakata, H.; Nomoto, K.; Kim, K.H.; Yongsiri, A.; Takeuchi, H. Isolation of achatin-I, a neuroactive tetrapeptide having a D-phenylalanine residue, from Achatina ganglia, and its effects on Achatina giant neurones. Comp. Biochem. Physiol. C 1991, 98, 97-103.
    • (1991) Comp. Biochem. Physiol. C , vol.98 , pp. 97-103
    • Kamatani, Y.1    Minakata, H.2    Nomoto, K.3    Kim, K.H.4    Yongsiri, A.5    Takeuchi, H.6
  • 166
    • 84869130235 scopus 로고    scopus 로고
    • Identification and characterization of a novel antimicrobial peptide from the venom of the ant Tetramorium bicarinatum
    • Rifflet, A.; Gavalda, S.; Tene, N.; Orivel, J.; Leprince, J.; Guilhaudis, L.; Genin, E.; Vetillard, A.; Treilhou, M. Identification and characterization of a novel antimicrobial peptide from the venom of the ant Tetramorium bicarinatum. Peptides 2012, 38, 363-370.
    • (2012) Peptides , vol.38 , pp. 363-370
    • Rifflet, A.1    Gavalda, S.2    Tene, N.3    Orivel, J.4    Leprince, J.5    Guilhaudis, L.6    Genin, E.7    Vetillard, A.8    Treilhou, M.9
  • 169
    • 0242637115 scopus 로고    scopus 로고
    • Cathelicidin family of antimicrobial peptides: Proteolytic processing and protease resistance
    • Shinnar, A.E.; Butler, K.L.; Park, H.J. Cathelicidin family of antimicrobial peptides: Proteolytic processing and protease resistance. Bioorg. Chem. 2003, 31, 425-436.
    • (2003) Bioorg. Chem. , vol.31 , pp. 425-436
    • Shinnar, A.E.1    Butler, K.L.2    Park, H.J.3
  • 171
    • 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
  • 172
    • 0034697120 scopus 로고    scopus 로고
    • Formation and characterization of a single trp-trp cross-link in indolicidin that confers protease stability without altering antimicrobial activity
    • Osapay, K.; Tran, D.; Ladokhin, A.S.; White, S.H.; Henschen, A.H.; Selsted, M.E. Formation and characterization of a single trp-trp cross-link in indolicidin that confers protease stability without altering antimicrobial activity. J. Biol. Chem. 2000, 275, 12017-12022.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12017-12022
    • Osapay, K.1    Tran, D.2    Ladokhin, A.S.3    White, S.H.4    Henschen, A.H.5    Selsted, M.E.6
  • 174
    • 0033594986 scopus 로고    scopus 로고
    • Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides
    • Zhang, L.; Benz, R.; Hancock, R.E. Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides. Biochemistry 1999, 38, 8102-8111.
    • (1999) Biochemistry , vol.38 , pp. 8102-8111
    • Zhang, L.1    Benz, R.2    Hancock, R.E.3
  • 175
    • 33645420007 scopus 로고    scopus 로고
    • Development of novel ll-37 derived antimicrobial peptides with LPS and LTA neutralizing and antimicrobial activities for therapeutic application
    • Nell, M.J.; Tjabringa, G.S.; Wafelman, A.R.; Verrijk, R.; Hiemstra, P.S.; Drijfhout, J.W.; Grote, J.J. Development of novel ll-37 derived antimicrobial peptides with LPS and LTA neutralizing and antimicrobial activities for therapeutic application. Peptides 2006, 27, 649-660.
    • (2006) Peptides , vol.27 , pp. 649-660
    • Nell, M.J.1    Tjabringa, G.S.2    Wafelman, A.R.3    Verrijk, R.4    Hiemstra, P.S.5    Drijfhout, J.W.6    Grote, J.J.7
  • 177
    • 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
  • 178
    • 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
  • 179
    • 78751575968 scopus 로고    scopus 로고
    • C-terminal amidation of pmap-23: Translocation to the inner membrane of gram-negative bacteria
    • Kim, J.Y.; Park, S.C.; Yoon, M.Y.; Hahm, K.S.; Park, Y. C-terminal amidation of pmap-23: Translocation to the inner membrane of gram-negative bacteria. Amino Acids 2011, 40, 183-195.
    • (2011) Amino Acids , vol.40 , pp. 183-195
    • Kim, J.Y.1    Park, S.C.2    Yoon, M.Y.3    Hahm, K.S.4    Park, Y.5
  • 181
    • 78650858133 scopus 로고    scopus 로고
    • De novo design of β-didehydrophenylalanine containing peptides: From models to applications
    • Gupta, M.; Chauhan, V.S. De novo design of β-didehydrophenylalanine containing peptides: From models to applications. Biopolymers 2011, 95, 161-173.
    • (2011) Biopolymers , vol.95 , pp. 161-173
    • Gupta, M.1    Chauhan, V.S.2
  • 182
    • 34247331353 scopus 로고    scopus 로고
    • Alpha, beta-dehydrophenylalanine containing cecropin-melittin hybrid peptides: Conformation and activity
    • Mathur, P.; Jagannathan, N.R.; Chauhan, V.S. Alpha, beta-dehydrophenylalanine containing cecropin-melittin hybrid peptides: Conformation and activity. J. Pept. Sci. 2007, 13, 253-262.
    • (2007) J. Pept. Sci. , vol.13 , pp. 253-262
    • Mathur, P.1    Jagannathan, N.R.2    Chauhan, V.S.3
  • 183
    • 77953200832 scopus 로고    scopus 로고
    • Synthesis and evaluation of new endomorphin-2 analogues containing (z)-alpha, beta-didehydrophenylalanine (delta(z)phe) residues
    • Torino, D.; Mollica, A.; Pinnen, F.; Feliciani, F.; Lucente, G.; Fabrizi, G.; Portalone, G.; Davis, P.; Lai, J.; Ma, S.W.; et al. Synthesis and evaluation of new endomorphin-2 analogues containing (z)-alpha, beta-didehydrophenylalanine (delta(z)phe) residues. J. Med. Chem. 2010, 53, 4550-4554.
    • (2010) J. Med. Chem. , vol.53 , pp. 4550-4554
    • Torino, D.1    Mollica, A.2    Pinnen, F.3    Feliciani, F.4    Lucente, G.5    Fabrizi, G.6    Portalone, G.7    Davis, P.8    Lai, J.9    Ma, S.W.10
  • 184
    • 0347625845 scopus 로고    scopus 로고
    • Bestowing antifungal and antibacterial activities by lipophilic acid conjugation to D, L-amino acid-containing antimicrobial peptides: A plausible mode of action
    • Avrahami, D.; Shai, Y. Bestowing antifungal and antibacterial activities by lipophilic acid conjugation to D, L-amino acid-containing antimicrobial peptides: A plausible mode of action. Biochemistry 2003, 42, 14946-14956.
    • (2003) Biochemistry , vol.42 , pp. 14946-14956
    • Avrahami, D.1    Shai, Y.2
  • 187
    • 29544441437 scopus 로고    scopus 로고
    • Evolutionary algorithms and de novo peptide design
    • Belda, I.; Llora, X.; Giralt, E. Evolutionary algorithms and de novo peptide design. Soft. Comput. 2006, 10, 295-304.
    • (2006) Soft. Comput. , vol.10 , pp. 295-304
    • Belda, I.1    Llora, X.2    Giralt, E.3
  • 188
    • 33750304297 scopus 로고    scopus 로고
    • A linguistic model for the rational design of antimicrobial peptides
    • Loose, C.; Jensen, K.; Rigoutsos, I.; Stephanopoulos, G. A linguistic model for the rational design of antimicrobial peptides. Nature 2006, 443, 867-869.
    • (2006) Nature , vol.443 , pp. 867-869
    • Loose, C.1    Jensen, K.2    Rigoutsos, I.3    Stephanopoulos, G.4
  • 189
    • 38849155828 scopus 로고    scopus 로고
    • QSAR modeling and computer-aided design of antimicrobial peptides
    • Jenssen, H.; Fjell, C.D.; Cherkasov, A.; Hancock, R.E. QSAR modeling and computer-aided design of antimicrobial peptides. J. Pept. Sci. 2008, 14, 110-114.
    • (2008) J. Pept. Sci. , vol.14 , pp. 110-114
    • Jenssen, H.1    Fjell, C.D.2    Cherkasov, A.3    Hancock, R.E.4
  • 190
    • 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. 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.8
  • 193
    • 0031451521 scopus 로고    scopus 로고
    • Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity
    • Tossi, A.; Tarantino, C.; Romeo, D. Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. Eur. J. Biochem. 1997, 250, 549-558.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 549-558
    • Tossi, A.1    Tarantino, C.2    Romeo, D.3
  • 194
    • 0028174888 scopus 로고
    • The nh2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity
    • Mor, A.; Nicolas, P. The nh2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity. J. Biol. Chem. 1994, 269, 1934-1939.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1934-1939
    • Mor, A.1    Nicolas, P.2
  • 195
    • 0028009472 scopus 로고
    • Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA
    • Storici, P.; Scocchi, M.; Tossi, A.; Gennaro, R.; Zanetti, M. Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA. FEBS Lett. 1994, 337, 303-307.
    • (1994) FEBS Lett. , vol.337 , pp. 303-307
    • Storici, P.1    Scocchi, M.2    Tossi, A.3    Gennaro, R.4    Zanetti, M.5
  • 196
    • 84882261077 scopus 로고    scopus 로고
    • In vitro activity of novel in silico-developed antimicrobial peptides against a panel of bacterial pathogens
    • Romani, A.A.; Baroni, M.C.; Taddei, S.; Ghidini, F.; Sansoni, P.; Cavirani, S.; Cabassi, C.S. In vitro activity of novel in silico-developed antimicrobial peptides against a panel of bacterial pathogens. J. Pept. Sci. 2013, 19, 554-565.
    • (2013) J. Pept. Sci. , vol.19 , pp. 554-565
    • Romani, A.A.1    Baroni, M.C.2    Taddei, S.3    Ghidini, F.4    Sansoni, P.5    Cavirani, S.6    Cabassi, C.S.7
  • 197
    • 84897368101 scopus 로고    scopus 로고
    • Design and activity of novel lactoferrampin analogues against O157:H7 enterohemorrhagic Escherichia coli
    • doi:10.1002/bip.22360
    • Cruz, J.; Ortiz, C.C.; Guzman, F.; Cardenas, C.; Fernandez-Lafuente, R.; Torres, R.G. Design and activity of novel lactoferrampin analogues against O157:H7 enterohemorrhagic Escherichia coli. Biopolymers 2013, doi:10.1002/bip.22360.
    • (2013) Biopolymers
    • Cruz, J.1    Ortiz, C.C.2    Guzman, F.3    Cardenas, C.4    Fernandez-Lafuente, R.5    Torres, R.G.6
  • 198
    • 1842483412 scopus 로고    scopus 로고
    • Treatment of infections associated with surgical implants
    • Darouiche, R.O. Treatment of infections associated with surgical implants. N. Engl. J. Med. 2004, 350, 1422-1429.
    • (2004) N. Engl. J. Med. , vol.350 , pp. 1422-1429
    • Darouiche, R.O.1
  • 199
    • 0035077009 scopus 로고    scopus 로고
    • Riddle of biofilm resistance
    • Lewis, K. Riddle of biofilm resistance. Antimicrob. Agents Chemother. 2001, 45, 999-1007.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 999-1007
    • Lewis, K.1
  • 201
    • 0035152224 scopus 로고    scopus 로고
    • Biofilm exopolysaccharides: A strong and sticky framework
    • Sutherland, I. Biofilm exopolysaccharides: A strong and sticky framework. Microbiology 2001, 147, 3-9.
    • (2001) Microbiology , vol.147 , pp. 3-9
    • Sutherland, I.1
  • 202
    • 0035014383 scopus 로고    scopus 로고
    • Mechanisms of biofilm resistance to antimicrobial agents
    • Mah, T.F.; O'Toole, G.A. Mechanisms of biofilm resistance to antimicrobial agents. Trends Microbiol. 2001, 9, 34-39.
    • (2001) Trends Microbiol. , vol.9 , pp. 34-39
    • Mah, T.F.1    O'Toole, G.A.2
  • 203
    • 0027441768 scopus 로고
    • Diffusion of rifampin and vancomycin through a Staphylococcus epidermidis biofilm
    • Dunne, W.M.; Mason, E.O.; Kaplan, S.L. Diffusion of rifampin and vancomycin through a Staphylococcus epidermidis biofilm. Antimicrob. Agents Chemother. 1993, 37, 2522-2526.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 2522-2526
    • Dunne, W.M.1    Mason, E.O.2    Kaplan, S.L.3
  • 205
    • 0035859467 scopus 로고    scopus 로고
    • Antibiotic resistance of bacteria in biofilms
    • Stewart, P.S.; Costerton, J.W. Antibiotic resistance of bacteria in biofilms. Lancet 2001, 358, 135-138.
    • (2001) Lancet , vol.358 , pp. 135-138
    • Stewart, P.S.1    Costerton, J.W.2
  • 206
    • 11844305018 scopus 로고    scopus 로고
    • Genomewide analysis of gene expression in Staphylococcus epidermidis biofilms: Insights into the pathophysiology of S. epidermidis biofilms and the role of phenol-soluble modulins in formation of biofilms
    • Yao, Y.; Sturdevant, D.E.; Otto, M. Genomewide analysis of gene expression in Staphylococcus epidermidis biofilms: Insights into the pathophysiology of S. epidermidis biofilms and the role of phenol-soluble modulins in formation of biofilms. J. Infect. Dis. 2005, 191, 289-298.
    • (2005) J. Infect. Dis. , vol.191 , pp. 289-298
    • Yao, Y.1    Sturdevant, D.E.2    Otto, M.3
  • 207
    • 33745206370 scopus 로고    scopus 로고
    • Bacterial evasion of antimicrobial peptides by biofilm formation
    • Otto, M. Bacterial evasion of antimicrobial peptides by biofilm formation. Curr. Top. Microbiol. Immunol. 2006, 306, 251-258.
    • (2006) Curr. Top. Microbiol. Immunol. , vol.306 , pp. 251-258
    • Otto, M.1
  • 208
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • Singh, P.K.; Parsek, M.R.; Greenberg, E.P.; Welsh, M.J. A component of innate immunity prevents bacterial biofilm development. Nature 2002, 417, 552-555.
    • (2002) Nature , vol.417 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 211
    • 79953029837 scopus 로고    scopus 로고
    • The biocompatibility and biofilm resistance of implant coatings based on hydrophilic polymer brushes conjugated with antimicrobial peptides
    • Gao, G.; Lange, D.; Hilpert, K.; Kindrachuk, J.; Zou, Y.; Cheng, J.T.; Kazemzadeh-Narbat, M.; Yu, K.; Wang, R.; Straus, S.K.; et al. The biocompatibility and biofilm resistance of implant coatings based on hydrophilic polymer brushes conjugated with antimicrobial peptides. Biomaterials 2011, 32, 3899-3909.
    • (2011) Biomaterials , vol.32 , pp. 3899-3909
    • Gao, G.1    Lange, D.2    Hilpert, K.3    Kindrachuk, J.4    Zou, Y.5    Cheng, J.T.6    Kazemzadeh-Narbat, M.7    Yu, K.8    Wang, R.9    Straus, S.K.10
  • 212
    • 0242592006 scopus 로고    scopus 로고
    • Gentamicin coating of metallic implants reduces implant-related osteomyelitis in rats
    • Lucke, M.; Schmidmaier, G.; Sadoni, S.; Wildemann, B.; Schiller, R.; Haas, N.P.; Raschke, M. Gentamicin coating of metallic implants reduces implant-related osteomyelitis in rats. Bone 2003, 32, 521-531.
    • (2003) Bone , vol.32 , pp. 521-531
    • Lucke, M.1    Schmidmaier, G.2    Sadoni, S.3    Wildemann, B.4    Schiller, R.5    Haas, N.P.6    Raschke, M.7
  • 213
    • 0030111319 scopus 로고    scopus 로고
    • Controlled release of antibiotics from coated orthopedic implants
    • Price, J.S.; Tencer, A.F.; Arm, D.M.; Bohach, G.A. Controlled release of antibiotics from coated orthopedic implants. J. Biomed. Mater. Res. 1996, 30, 281-286.
    • (1996) J. Biomed. Mater. Res. , vol.30 , pp. 281-286
    • Price, J.S.1    Tencer, A.F.2    Arm, D.M.3    Bohach, G.A.4
  • 214
    • 0037338940 scopus 로고    scopus 로고
    • Antibacterial poly(D, L-lactic acid) coating of medical implants using a biodegradable drug delivery technology
    • Gollwitzer, H.; Ibrahim, K.; Meyer, H.; Mittelmeier, W.; Busch, R.; Stemberger, A. Antibacterial poly(D, L-lactic acid) coating of medical implants using a biodegradable drug delivery technology. J. Antimicrob. Chemoth. 2003, 51, 585-591.
    • (2003) J. Antimicrob. Chemoth. , vol.51 , pp. 585-591
    • Gollwitzer, H.1    Ibrahim, K.2    Meyer, H.3    Mittelmeier, W.4    Busch, R.5    Stemberger, A.6
  • 215
    • 77951014179 scopus 로고    scopus 로고
    • Prevention of biofilm formation on titanium surfaces modified with conjugated molecules comprised of antimicrobial and titanium-binding peptides
    • Yoshinari, M.; Kato, T.; Matsuzaka, K.; Hayakawa, T.; Shiba, K. Prevention of biofilm formation on titanium surfaces modified with conjugated molecules comprised of antimicrobial and titanium-binding peptides. Biofouling 2010, 26, 103-110.
    • (2010) Biofouling , vol.26 , pp. 103-110
    • Yoshinari, M.1    Kato, T.2    Matsuzaka, K.3    Hayakawa, T.4    Shiba, K.5
  • 217
    • 33749170651 scopus 로고    scopus 로고
    • Effect of muc7 peptides on the growth of bacteria and on Streptococcus mutans biofilm
    • Wei, G.X.; Campagna, A.N.; Bobek, L.A. Effect of muc7 peptides on the growth of bacteria and on Streptococcus mutans biofilm. J. Antimicrob. Chemother. 2006, 57, 1100-1109.
    • (2006) J. Antimicrob. Chemother. , vol.57 , pp. 1100-1109
    • Wei, G.X.1    Campagna, A.N.2    Bobek, L.A.3
  • 219
    • 0030741702 scopus 로고    scopus 로고
    • Permeation of antimicrobial agents through Pseudomonas aeruginosa biofilms: A simple method
    • Shigeta, M.; Tanaka, G.; Komatsuzawa, H.; Sugai, M.; Suginaka, H.; Usui, T. Permeation of antimicrobial agents through Pseudomonas aeruginosa biofilms: A simple method. Chemotherapy 1997, 43, 340-345.
    • (1997) Chemotherapy , vol.43 , pp. 340-345
    • Shigeta, M.1    Tanaka, G.2    Komatsuzawa, H.3    Sugai, M.4    Suginaka, H.5    Usui, T.6
  • 220
    • 36849039966 scopus 로고    scopus 로고
    • Tuning the membrane selectivity of antimicrobial peptides by using multivalent design
    • Liu, Z.G.; Young, A.W.; Hu, P.; Rice, A.J.; Zhou, C.H.; Zhan, Y.K.; 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.G.1    Young, A.W.2    Hu, P.3    Rice, A.J.4    Zhou, C.H.5    Zhan, Y.K.6    Kallenbach, N.R.7
  • 222
    • 77749245787 scopus 로고    scopus 로고
    • Effects of trp-and arg-containing antimicrobial-peptide structure on inhibition of Escherichia coli planktonic growth and biofilm formation
    • Hou, S.; Liu, Z.; Young, A.W.; Mark, S.L.; Kallenbach, N.R.; Ren, D. Effects of trp-and arg-containing antimicrobial-peptide structure on inhibition of Escherichia coli planktonic growth and biofilm formation. Appl. Environ. Microbiol. 2010, 76, 1967-1974.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 1967-1974
    • Hou, S.1    Liu, Z.2    Young, A.W.3    Mark, S.L.4    Kallenbach, N.R.5    Ren, D.6
  • 224
    • 84884227799 scopus 로고    scopus 로고
    • Antimicrobial peptide gl13k is effective in reducing biofilms of Pseudomonas aeruginosa
    • Hirt, H.; Gorr, S.U. Antimicrobial peptide gl13k is effective in reducing biofilms of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 2013, 57, 4903-4910.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 4903-4910
    • Hirt, H.1    Gorr, S.U.2
  • 225
    • 84879478218 scopus 로고    scopus 로고
    • Anti-microbial, anti-biofilm activities and cell selectivity of the nrc-16 peptide derived from witch flounder, Glyptocephalus cynoglossus
    • Gopal, R.; Lee, J.H.; Kim, Y.G.; Kim, M.S.; Seo, C.H.; Park, Y. Anti-microbial, anti-biofilm activities and cell selectivity of the nrc-16 peptide derived from witch flounder, Glyptocephalus cynoglossus. Mar. Drugs 2013, 11, 1836-1852.
    • (2013) Mar. Drugs , vol.11 , pp. 1836-1852
    • Gopal, R.1    Lee, J.H.2    Kim, Y.G.3    Kim, M.S.4    Seo, C.H.5    Park, Y.6
  • 226
    • 0032991901 scopus 로고    scopus 로고
    • Lactoferrin increases the susceptibility of S. epidermidis biofilms to lysozyme and vancomycin
    • Leitch, E.C.; Willcox, M.D. Lactoferrin increases the susceptibility of S. epidermidis biofilms to lysozyme and vancomycin. Curr. Eye Res. 1999, 19, 12-19.
    • (1999) Curr. Eye Res. , vol.19 , pp. 12-19
    • Leitch, E.C.1    Willcox, M.D.2
  • 227
    • 77955628762 scopus 로고    scopus 로고
    • Persister cells
    • Lewis, K. Persister cells. Annu. Rev. Microbiol. 2010, 64, 357-372.
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 357-372
    • Lewis, K.1
  • 228
    • 79961095617 scopus 로고    scopus 로고
    • Control of bacterial persister cells by trp/arg-containing antimicrobial peptides
    • Chen, X.; Zhang, M.; Zhou, C.; Kallenbach, N.R.; Ren, D. Control of bacterial persister cells by trp/arg-containing antimicrobial peptides. Appl. Environ. Microbiol. 2011, 77, 4878-4885.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 4878-4885
    • Chen, X.1    Zhang, M.2    Zhou, C.3    Kallenbach, N.R.4    Ren, D.5
  • 229
    • 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
  • 230
    • 62449140880 scopus 로고    scopus 로고
    • Phosphoethanolamine substitution of lipid a and resistance of Neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serum
    • Lewis, L.A.; Choudhury, B.; Balthazar, J.T.; Martin, L.E.; Ram, S.; Rice, P.A.; Stephens, D.S.; Carlson, R.; Shafer, W.M. Phosphoethanolamine substitution of lipid a and resistance of Neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serum. Infect. Immun. 2009, 77, 1112-1120.
    • (2009) Infect. Immun. , vol.77 , pp. 1112-1120
    • Lewis, L.A.1    Choudhury, B.2    Balthazar, J.T.3    Martin, L.E.4    Ram, S.5    Rice, P.A.6    Stephens, D.S.7    Carlson, R.8    Shafer, W.M.9
  • 231
    • 0034985868 scopus 로고    scopus 로고
    • Bacterial modification of LPS and resistance to antimicrobial peptides
    • Gunn, J.S. Bacterial modification of LPS and resistance to antimicrobial peptides. J. Endotoxin Res. 2001, 7, 57-62.
    • (2001) J. Endotoxin Res. , vol.7 , pp. 57-62
    • Gunn, J.S.1
  • 232
    • 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
  • 233
    • 0033919460 scopus 로고    scopus 로고
    • A phop-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides
    • Guina, T.; Yi, E.C.; Wang, H.; Hackett, M.; Miller, S.I. A phop-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides. J. Bacteriol. 2000, 182, 4077-4086.
    • (2000) J. Bacteriol. , vol.182 , pp. 4077-4086
    • Guina, T.1    Yi, E.C.2    Wang, H.3    Hackett, M.4    Miller, S.I.5
  • 234
    • 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.; 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.2    Waring, A.J.3    Lehrer, R.I.4
  • 235
    • 0035101015 scopus 로고    scopus 로고
    • Construction and characterization of mutations at codon 751 of the Escherichia coli gyrB gene that confer resistance to the antimicrobial peptide microcin b17 and alter the activity of DNA gyrase
    • Del Castillo, F.J.; del Castillo, I.; Moreno, F. Construction and characterization of mutations at codon 751 of the Escherichia coli gyrB gene that confer resistance to the antimicrobial peptide microcin b17 and alter the activity of DNA gyrase. J. Bacteriol. 2001, 183, 2137-2140.
    • (2001) J. Bacteriol. , vol.183 , pp. 2137-2140
    • Del Castillo, F.J.1    del Castillo, I.2    Moreno, F.3
  • 237
    • 0031984629 scopus 로고    scopus 로고
    • Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action
    • Yeaman, M.R.; Bayer, A.S.; Koo, S.P.; Foss, W.; Sullam, P.M. Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action. J. Clin. Invest. 1998, 101, 178-187.
    • (1998) J. Clin. Invest. , vol.101 , pp. 178-187
    • Yeaman, M.R.1    Bayer, A.S.2    Koo, S.P.3    Foss, W.4    Sullam, P.M.5
  • 238
    • 1342304447 scopus 로고    scopus 로고
    • Polysaccharide intercellular adhesin (pia) protects Staphylococcus epidermidis against major components of the human innate immune system
    • Vuong, C.; Voyich, J.M.; Fischer, E.R.; Braughton, K.R.; Whitney, A.R.; DeLeo, F.R.; Otto, M. Polysaccharide intercellular adhesin (pia) protects Staphylococcus epidermidis against major components of the human innate immune system. Cell Microbiol. 2004, 6, 269-275.
    • (2004) Cell Microbiol. , vol.6 , pp. 269-275
    • Vuong, C.1    Voyich, J.M.2    Fischer, E.R.3    Braughton, K.R.4    Whitney, A.R.5    DeLeo, F.R.6    Otto, M.7
  • 239
    • 0003582512 scopus 로고
    • A two-component regulatory system (phop phoq) controls Salmonella typhimurium virulence
    • Miller, S.I.; Kukral, A.M.; Mekalanos, J.J. A two-component regulatory system (phop phoq) controls Salmonella typhimurium virulence. Proc. Natl. Acad. Sci. USA 1989, 86, 5054-5058.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.