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Volumn 92, Issue 9, 2010, Pages 1236-1241

Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity

Author keywords

Antimicrobial peptides; Antimicrobial resistance; Host defense peptides; Structure activity relationship

Indexed keywords

ANTIMICROBIAL ACTIVITY; HOST RESISTANCE; HYDROPHOBICITY; IMMUNITY; NONHUMAN; PHYSICAL CHEMISTRY; REVIEW;

EID: 77955846576     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.02.023     Document Type: Review
Times cited : (271)

References (79)
  • 2
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock R.E., Sahl H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 2006, 24:1551-1557.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 3
    • 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
  • 5
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • Peschel A., Sahl H.G. The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev. Microbiol. 2006, 4:529-536.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 7
    • 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
  • 8
    • 20544442905 scopus 로고    scopus 로고
    • Alarmins: chemotactic activators of immune responses
    • Oppenheim J.J., Yang D. Alarmins: chemotactic activators of immune responses. Curr. Opin. Immunol. 2005, 17:359-365.
    • (2005) Curr. Opin. Immunol. , vol.17 , pp. 359-365
    • Oppenheim, J.J.1    Yang, D.2
  • 9
    • 69949086979 scopus 로고    scopus 로고
    • Potential of immunomodulatory host defense peptides as novel anti-infectives
    • Easton D.M., Nijnik A., Mayer M.L., Hancock R.E. Potential of immunomodulatory host defense peptides as novel anti-infectives. Trends Biotechnol. 2009, 27:582-590.
    • (2009) Trends Biotechnol. , vol.27 , pp. 582-590
    • Easton, D.M.1    Nijnik, A.2    Mayer, M.L.3    Hancock, R.E.4
  • 10
    • 0036257512 scopus 로고    scopus 로고
    • Molecular diversity in gene-encoded, cationic antimicrobial polypeptides
    • Tossi A., Sandri L. Molecular diversity in gene-encoded, cationic antimicrobial polypeptides. Curr. Pharm. Des. 2002, 8:743-761.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 743-761
    • Tossi, A.1    Sandri, L.2
  • 11
    • 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
  • 12
    • 57749088664 scopus 로고    scopus 로고
    • Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles
    • Wang G. Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J. Biol. Chem. 2008, 283:32637-32643.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32637-32643
    • Wang, G.1
  • 13
    • 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
  • 14
    • 0020479083 scopus 로고
    • The structure of melittin. I. Structure determination and partial refinement
    • Terwilliger T.C., Eisenberg D. The structure of melittin. I. Structure determination and partial refinement. J. Biol. Chem. 1982, 257:6010-6015.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 15
    • 0020479123 scopus 로고
    • The structure of melittin. II. Interpretation of the structure
    • Terwilliger T.C., Eisenberg D. The structure of melittin. II. Interpretation of the structure. J. Biol. Chem. 1982, 257:6016-6022.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6016-6022
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 16
    • 0031062621 scopus 로고    scopus 로고
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. J. Biomol. NMR 1997, 9:127-135.
    • (1997) J. Biomol. NMR , vol.9 , pp. 127-135
    • Gesell, J.1    Zasloff, M.2    Opella, S.J.3
  • 17
    • 33745266360 scopus 로고    scopus 로고
    • Structure-activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken
    • Xiao Y., Dai H., Bommineni Y.R., Soulages J.L., Gong Y.X., Prakash O., Zhang G. Structure-activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken. FEBS J. 2006, 273:2581-2593.
    • (2006) FEBS J. , vol.273 , pp. 2581-2593
    • Xiao, Y.1    Dai, H.2    Bommineni, Y.R.3    Soulages, J.L.4    Gong, Y.X.5    Prakash, O.6    Zhang, G.7
  • 18
    • 77952546164 scopus 로고    scopus 로고
    • The Central kink region of fowlicidin-2, an alpha-helical host defense peptide, is critically involved in bacterial killing and endotoxin neutralization
    • Xiao Y., Herrera A.I., Bommineni Y.R., Soulages J.L., Prakash O., Zhang G. The Central kink region of fowlicidin-2, an alpha-helical host defense peptide, is critically involved in bacterial killing and endotoxin neutralization. J. Innate Immun. 2009, 1:268-280.
    • (2009) J. Innate Immun. , vol.1 , pp. 268-280
    • Xiao, Y.1    Herrera, A.I.2    Bommineni, Y.R.3    Soulages, J.L.4    Prakash, O.5    Zhang, G.6
  • 19
    • 33846006520 scopus 로고    scopus 로고
    • Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities
    • Bommineni Y.R., Dai H., Gong Y.X., Soulages J.L., Fernando S.C., Desilva U., Prakash O., Zhang G. Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities. FEBS J. 2007, 274:418-428.
    • (2007) FEBS J. , vol.274 , pp. 418-428
    • Bommineni, Y.R.1    Dai, H.2    Gong, Y.X.3    Soulages, J.L.4    Fernando, S.C.5    Desilva, U.6    Prakash, O.7    Zhang, G.8
  • 20
    • 33745855891 scopus 로고    scopus 로고
    • Membrane-bound dimer structure of a beta-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR
    • Mani R., Tang M., Wu X., Buffy J.J., Waring A.J., Sherman M.A., Hong M. Membrane-bound dimer structure of a beta-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR. Biochemistry 2006, 45:8341-8349.
    • (2006) Biochemistry , vol.45 , pp. 8341-8349
    • Mani, R.1    Tang, M.2    Wu, X.3    Buffy, J.J.4    Waring, A.J.5    Sherman, M.A.6    Hong, M.7
  • 21
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: antimicrobial peptides of innate immunity
    • Ganz T. Defensins: antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 2003, 3:710-720.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 710-720
    • Ganz, T.1
  • 23
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted M.E., Ouellette A.J. Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 2005, 6:551-557.
    • (2005) Nat. Immunol. , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 24
    • 9144261231 scopus 로고    scopus 로고
    • A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins
    • Xiao Y., Hughes A.L., Ando J., Matsuda Y., Cheng J.F., Skinner-Noble D., Zhang G. A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins. BMC Genomics 2004, 5:56.
    • (2004) BMC Genomics , vol.5 , pp. 56
    • Xiao, Y.1    Hughes, A.L.2    Ando, J.3    Matsuda, Y.4    Cheng, J.F.5    Skinner-Noble, D.6    Zhang, G.7
  • 25
    • 14644435363 scopus 로고    scopus 로고
    • Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes
    • Patil A., Hughes A.L., Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. Physiol. Genomics 2004, 20:1-11.
    • (2004) Physiol. Genomics , vol.20 , pp. 1-11
    • Patil, A.1    Hughes, A.L.2    Zhang, G.3
  • 26
    • 33645469217 scopus 로고    scopus 로고
    • Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract
    • Patil A.A., Cai Y., Sang Y., Blecha F., Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. Physiol. Genomics 2005, 23:5-17.
    • (2005) Physiol. Genomics , vol.23 , pp. 5-17
    • Patil, A.A.1    Cai, Y.2    Sang, Y.3    Blecha, F.4    Zhang, G.5
  • 27
    • 33751545243 scopus 로고    scopus 로고
    • Crystal structures of human alpha-defensins HNP4, HD5, and HD6
    • Szyk A., Wu Z., Tucker K., Yang D., Lu W., Lubkowski J. Crystal structures of human alpha-defensins HNP4, HD5, and HD6. Protein Sci. 2006, 15:2749-2760.
    • (2006) Protein Sci. , vol.15 , pp. 2749-2760
    • Szyk, A.1    Wu, Z.2    Tucker, K.3    Yang, D.4    Lu, W.5    Lubkowski, J.6
  • 28
    • 30044432598 scopus 로고    scopus 로고
    • Why is the Arg5-Glu13 salt bridge conserved in mammalian alpha-defensins?
    • Wu Z., Li X., de Leeuw E., Ericksen B., Lu W. Why is the Arg5-Glu13 salt bridge conserved in mammalian alpha-defensins?. J. Biol. Chem. 2005, 280:43039-43047.
    • (2005) J. Biol. Chem. , vol.280 , pp. 43039-43047
    • Wu, Z.1    Li, X.2    de Leeuw, E.3    Ericksen, B.4    Lu, W.5
  • 30
    • 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
  • 31
    • 0033592961 scopus 로고    scopus 로고
    • Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold
    • Schibli D.J., Hwang P.M., Vogel H.J. Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold. Biochemistry 1999, 38:16749-16755.
    • (1999) Biochemistry , vol.38 , pp. 16749-16755
    • Schibli, D.J.1    Hwang, P.M.2    Vogel, H.J.3
  • 32
    • 0023888810 scopus 로고
    • Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans
    • Oppenheim F.G., Xu T., McMillian F.M., Levitz S.M., Diamond R.D., Offner G.D., Troxler R.F. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J. Biol. Chem. 1988, 263:7472-7477.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7472-7477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3    Levitz, S.M.4    Diamond, R.D.5    Offner, G.D.6    Troxler, R.F.7
  • 33
    • 0026349223 scopus 로고
    • Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides
    • Agerberth B., Lee J.Y., Bergman T., Carlquist M., Boman H.G., Mutt V., Jornvall H. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur. J. Biochem. 1991, 202:849-854.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 849-854
    • Agerberth, B.1    Lee, J.Y.2    Bergman, T.3    Carlquist, M.4    Boman, H.G.5    Mutt, V.6    Jornvall, H.7
  • 34
    • 0028585933 scopus 로고
    • Identification of a proline-arginine-rich antibacterial peptide from neutrophils that is analogous to PR-39, an antibacterial peptide from the small intestine
    • Shi J., Ross C.R., Chengappa M.M., Blecha F. Identification of a proline-arginine-rich antibacterial peptide from neutrophils that is analogous to PR-39, an antibacterial peptide from the small intestine. J. Leukoc. Biol. 1994, 56:807-811.
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 807-811
    • Shi, J.1    Ross, C.R.2    Chengappa, M.M.3    Blecha, F.4
  • 36
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • De Y., Chen Q., Schmidt A.P., Anderson G.M., Wang J.M., Wooters J., Oppenheim J.J., Chertov O. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 2000, 192:1069-1074.
    • (2000) J. Exp. Med. , vol.192 , pp. 1069-1074
    • De, Y.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 38
    • 1842581655 scopus 로고    scopus 로고
    • A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release
    • Elssner A., Duncan M., Gavrilin M., Wewers M.D. A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release. J. Immunol. 2004, 172:4987-4994.
    • (2004) J. Immunol. , vol.172 , pp. 4987-4994
    • Elssner, A.1    Duncan, M.2    Gavrilin, M.3    Wewers, M.D.4
  • 39
    • 0346996865 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor
    • Tjabringa G.S., Aarbiou J., Ninaber D.K., Drijfhout J.W., Sorensen O.E., Borregaard N., Rabe K.F., Hiemstra P.S. The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J. Immunol. 2003, 171:6690-6696.
    • (2003) J. Immunol. , vol.171 , pp. 6690-6696
    • Tjabringa, G.S.1    Aarbiou, J.2    Ninaber, D.K.3    Drijfhout, J.W.4    Sorensen, O.E.5    Borregaard, N.6    Rabe, K.F.7    Hiemstra, P.S.8
  • 43
    • 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
  • 44
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action
    • Chan D.I., Prenner E.J., Vogel H.J. Tryptophan- and arginine-rich 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
  • 47
    • 0032738115 scopus 로고    scopus 로고
    • Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin
    • Miteva M., Andersson M., Karshikoff A., Otting G. Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin. FEBS Lett. 1999, 462:155-158.
    • (1999) FEBS Lett. , vol.462 , pp. 155-158
    • Miteva, M.1    Andersson, M.2    Karshikoff, A.3    Otting, G.4
  • 48
    • 3042818271 scopus 로고    scopus 로고
    • Kinetics of dye efflux and lipid flip-flop induced by delta-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, alpha-helical peptides
    • Pokorny A., Almeida P.F. Kinetics of dye efflux and lipid flip-flop induced by delta-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, alpha-helical peptides. Biochemistry 2004, 43:8846-8857.
    • (2004) Biochemistry , vol.43 , pp. 8846-8857
    • Pokorny, A.1    Almeida, P.F.2
  • 49
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1999, 1462:71-87.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 50
    • 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
  • 51
    • 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
  • 52
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • Dathe M., Nikolenko H., Meyer J., Beyermann M., Bienert M. Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Lett. 2001, 501:146-150.
    • (2001) FEBS Lett. , vol.501 , pp. 146-150
    • Dathe, M.1    Nikolenko, H.2    Meyer, J.3    Beyermann, M.4    Bienert, M.5
  • 53
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus
    • Schibli D.J., Hunter H.N., Aseyev V., Starner T.D., Wiencek J.M., McCray P.B., Tack B.F., Vogel H.J. The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. J. Biol. Chem. 2002, 277:8279-8289.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray, P.B.6    Tack, B.F.7    Vogel, H.J.8
  • 54
    • 0030664760 scopus 로고    scopus 로고
    • Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment
    • Wieprecht T., Dathe M., Krause E., Beyermann M., Maloy W.L., MacDonald D.L., Bienert M. Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment. FEBS Lett. 1997, 417:135-140.
    • (1997) FEBS Lett. , vol.417 , pp. 135-140
    • Wieprecht, T.1    Dathe, M.2    Krause, E.3    Beyermann, M.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7
  • 55
    • 0033532175 scopus 로고    scopus 로고
    • Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity
    • Kondejewski L.H., Jelokhani-Niaraki M., Farmer S.W., Lix B., Kay C.M., Sykes B.D., Hancock R.E., Hodges R.S. Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity. J. Biol. Chem. 1999, 274:13181-13192.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13181-13192
    • Kondejewski, L.H.1    Jelokhani-Niaraki, M.2    Farmer, S.W.3    Lix, B.4    Kay, C.M.5    Sykes, B.D.6    Hancock, R.E.7    Hodges, R.S.8
  • 56
    • 0030957876 scopus 로고    scopus 로고
    • Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes
    • Wieprecht T., Dathe M., Beyermann M., Krause E., Maloy W.L., MacDonald D.L., Bienert M. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry 1997, 36:6124-6132.
    • (1997) Biochemistry , vol.36 , pp. 6124-6132
    • Wieprecht, T.1    Dathe, M.2    Beyermann, M.3    Krause, E.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7
  • 59
    • 39149127361 scopus 로고    scopus 로고
    • Structure-activity relationships in beta-defensin peptides
    • Taylor K., Barran P.E., Dorin J.R. Structure-activity relationships in beta-defensin peptides. Biopolymers 2008, 90:1-7.
    • (2008) Biopolymers , vol.90 , pp. 1-7
    • Taylor, K.1    Barran, P.E.2    Dorin, J.R.3
  • 60
    • 0036171208 scopus 로고    scopus 로고
    • Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: structural and disulfide bridge requirements for activity
    • Mandal M., Jagannadham M.V., Nagaraj R. Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: structural and disulfide bridge requirements for activity. Peptides 2002, 23:413-418.
    • (2002) Peptides , vol.23 , pp. 413-418
    • Mandal, M.1    Jagannadham, M.V.2    Nagaraj, R.3
  • 62
    • 22244480342 scopus 로고    scopus 로고
    • Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity
    • Kluver E., Schulz-Maronde S., Scheid S., Meyer B., Forssmann W.G., Adermann K. Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity. Biochemistry 2005, 44:9804-9816.
    • (2005) Biochemistry , vol.44 , pp. 9804-9816
    • Kluver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.G.5    Adermann, K.6
  • 64
    • 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
  • 65
    • 0030033588 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp
    • Dougherty D.A. Cation-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
  • 69
    • 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
  • 70
    • 65449153221 scopus 로고    scopus 로고
    • End-tagging of ultra-short antimicrobial peptides by W/F stretches to facilitate bacterial killing
    • Pasupuleti M., Schmidtchen A., Chalupka A., Ringstad L., Malmsten M. End-tagging of ultra-short antimicrobial peptides by W/F stretches to facilitate bacterial killing. PLoS One 2009, 4:e5285.
    • (2009) PLoS One , vol.4
    • Pasupuleti, M.1    Schmidtchen, A.2    Chalupka, A.3    Ringstad, L.4    Malmsten, M.5
  • 72
    • 0031696867 scopus 로고    scopus 로고
    • Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data
    • Mandard N., Sodano P., Labbe H., Bonmatin J.M., Bulet P., Hetru C., Ptak M., Vovelle F. Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data. Eur. J. Biochem. 1998, 256:404-410.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 404-410
    • Mandard, N.1    Sodano, P.2    Labbe, H.3    Bonmatin, J.M.4    Bulet, P.5    Hetru, C.6    Ptak, M.7    Vovelle, F.8
  • 73
    • 0037108278 scopus 로고    scopus 로고
    • Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives
    • Laederach A., Andreotti A.H., Fulton D.B. Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives. Biochemistry 2002, 41:12359-12368.
    • (2002) Biochemistry , vol.41 , pp. 12359-12368
    • Laederach, A.1    Andreotti, A.H.2    Fulton, D.B.3
  • 74
    • 0030198873 scopus 로고    scopus 로고
    • Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes
    • Fahrner R.L., Dieckmann T., Harwig S.S., Lehrer R.I., Eisenberg D., Feigon J. Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes. Chem. Biol. 1996, 3:543-550.
    • (1996) Chem. Biol. , vol.3 , pp. 543-550
    • Fahrner, R.L.1    Dieckmann, T.2    Harwig, S.S.3    Lehrer, R.I.4    Eisenberg, D.5    Feigon, J.6
  • 75
    • 34250887046 scopus 로고    scopus 로고
    • Structure-based protein engineering for alpha-amylase inhibitory activity of plant defensin
    • Lin K.F., Lee T.R., Tsai P.H., Hsu M.P., Chen C.S., Lyu P.C. Structure-based protein engineering for alpha-amylase inhibitory activity of plant defensin. Proteins 2007, 68:530-540.
    • (2007) Proteins , vol.68 , pp. 530-540
    • Lin, K.F.1    Lee, T.R.2    Tsai, P.H.3    Hsu, M.P.4    Chen, C.S.5    Lyu, P.C.6
  • 78
    • 0025903814 scopus 로고
    • Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization
    • Hill C.P., Yee J., Selsted M.E., Eisenberg D. Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. Science 1991, 251:1481-1485.
    • (1991) Science , vol.251 , pp. 1481-1485
    • Hill, C.P.1    Yee, J.2    Selsted, M.E.3    Eisenberg, D.4


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