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Volumn 19, Issue 7, 2003, Pages 735-740

Research advances in cationic antimicrobial peptides

Author keywords

Activities; Cationic antimicrobial peptides; Mode of action; Recombinant production; Structure; Structure function relationships

Indexed keywords

ANTIINFECTIVE AGENT; PEPTIDE;

EID: 0041660859     PISSN: 10011978     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (44)
  • 1
    • 0032903987 scopus 로고    scopus 로고
    • The human cationic antimicrobial protein (hCAP18), a peptide antibiotic, Is widely expressed in human squamous epithelia and colocalizes with interleukin-6
    • Nilsson MF, Soandstedt B, Sorensen O et al. The human cationic antimicrobial protein (hCAP18), a peptide antibiotic, Is widely expressed in human squamous epithelia and colocalizes with interleukin-6. Infection and Immunity, 1999;67(5):2561-6
    • (1999) Infection and Immunity , vol.67 , Issue.5 , pp. 2561-2566
    • Nilsson, M.F.1    Soandstedt, B.2    Sorensen, O.3
  • 2
    • 0034806944 scopus 로고    scopus 로고
    • RL-37, an alpha- helical antimicrobial peptide of the rhesus monkey
    • Zhao C, Nguyen T, Boo LM et al. RL-37, an alpha- helical antimicrobial peptide of the rhesus monkey. Antimicrobial Agents and Chemotherapy, 2001;45(10):2695-702
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.10 , pp. 2695-2702
    • Zhao, C.1    Nguyen, T.2    Boo, L.M.3
  • 3
    • 0035038578 scopus 로고    scopus 로고
    • Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin
    • Pat rzykat A, Zhang L, Mendoza V et al. Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin. Antimicrobial Agents and Chemotherapy, 2001;45 (5):1337-42
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.5 , pp. 1337-1342
    • Patrzykat, A.1    Zhang, L.2    Mendoza, V.3
  • 4
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock REW, Scott MG. The role of antimicrobial peptides in animal defenses. Proc. Natl Acad Sci USA, 2000;97(16): 8856-61
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.16 , pp. 8856-8861
    • Hancock, R.E.W.1    Scott, M.G.2
  • 5
    • 0036707998 scopus 로고    scopus 로고
    • Plasticity in structure and interactions is critical for the action of indolicidin, an antibacterial peptide of innate immune origin
    • Nagpal S, Kaur KJ, Jain D, Salunke DM. Plasticity in structure and interactions is critical for the action of indolicidin, an antibacterial peptide of innate immune origin. Protein Sci, 2002;11 (9):2158-67
    • (2002) Protein Sci , vol.11 , Issue.9 , pp. 2158-2167
    • Nagpal, S.1    Kaur, K.J.2    Jain, D.3    Salunke, D.M.4
  • 6
    • 0036151109 scopus 로고    scopus 로고
    • Cell differentiation is a key determinant of cathelicidin LL-37/Human cationic antimicrobial protein 18 expression by human colon epithelium
    • Hase K, Eckmann L, Leopard JD et al. Cell differentiation is a key determinant of cathelicidin LL-37/Human cationic antimicrobial protein 18 expression by human colon epithelium. Infection and Immunity, 2002;70(2):953-1063
    • (2002) Infection and Immunity , vol.70 , Issue.2 , pp. 953-1063
    • Hase, K.1    Eckmann, L.2    Leopard, J.D.3
  • 7
    • 0033915249 scopus 로고    scopus 로고
    • Characterization of a fish antimicrobial peptide: Gene expression, subcellular localization, and spectrum of activity
    • Cole AM, Darouiche RO, Legarda D et al. Characterization of a fish antimicrobial peptide: Gene expression, subcellular localization, and spectrum of activity. Antimicrobial Agents and Chemotherapy, 2000;44(8):2039-45
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.8 , pp. 2039-2045
    • Cole, A.M.1    Darouiche, R.O.2    Legarda, D.3
  • 8
    • 0033981142 scopus 로고    scopus 로고
    • Transcriptional regulation of beta-defensin gene expression in tracheal epithelial cells
    • Diamond G, Kaiser V, Rhodes J et al. Transcriptional regulation of beta-defensin gene expression in tracheal epithelial cells. Infect Immun, 2000;68(1):113-9
    • (2000) Infect Immun , vol.68 , Issue.1 , pp. 113-119
    • Diamond, G.1    Kaiser, V.2    Rhodes, J.3
  • 9
    • 0034697731 scopus 로고    scopus 로고
    • Structural organization and expression of the gaegurin 4 gene of Rana rugosa
    • Kwon SY, Carlson BA, Park JM, Lee BJ. Structural organization and expression of the gaegurin 4 gene of Rana rugosa. Biochim Biophys Acta, 2000;1492(1):185-90
    • (2000) Biochim Biophys Acta , vol.1492 , Issue.1 , pp. 185-190
    • Kwon, S.Y.1    Carlson, B.A.2    Park, J.M.3    Lee, B.J.4
  • 10
    • 0032885379 scopus 로고    scopus 로고
    • In vitro activity of polycationic peptides against cryptosporidium parvum, pneumocystis carinii and yeast clinical isolates
    • Giacometti A, Cirioni O, Barchiesi F et al. In vitro activity of polycationic peptides against cryptosporidium parvum, pneumocystis carinii and yeast clinical isolates. J Antimicrob Chemother, 1999;44(3):403-6
    • (1999) J Antimicrob Chemother , vol.44 , Issue.3 , pp. 403-406
    • Giacometti, A.1    Cirioni, O.2    Barchiesi, F.3
  • 11
    • 0033003473 scopus 로고    scopus 로고
    • Biological properties of structurally related α-helical cationic antimicrobial peptides
    • Scott MG, Yan H, Hancock REW. Biological properties of structurally related α-helical cationic antimicrobial peptides. Infection and Immunity, 1999;67(4):2005-9
    • (1999) Infection and Immunity , vol.67 , Issue.4 , pp. 2005-2009
    • Scott, M.G.1    Yan, H.2    Hancock, R.E.W.3
  • 12
    • 0036796148 scopus 로고    scopus 로고
    • Isolation of human cationic antimicrobial protein-18 from seminal plasma and its association with prostasomes
    • Andersson E, Sorensen OE, Frohm B et al. Isolation of human cationic antimicrobial protein-18 from seminal plasma and its association with prostasomes. Hum Reprod, 2002;17(10):2529 -34
    • (2002) Hum Reprod , vol.17 , Issue.10 , pp. 2529-2534
    • Andersson, E.1    Sorensen, O.E.2    Frohm, B.3
  • 13
    • 0033560645 scopus 로고    scopus 로고
    • Transfer of a cathelicidin peptide antibiotic gene restores bacterial killing in a cystic fibrosis xenograft model
    • Bals R, Weine DJ, Meegalla RI, Wilson JM. Transfer of a cathelicidin peptide antibiotic gene restores bacterial killing in a cystic fibrosis xenograft model. J Clin Invest, 1999;103(8): 1113-7
    • (1999) J Clin Invest , vol.103 , Issue.8 , pp. 1113-1117
    • Bals, R.1    Weine, D.J.2    Meegalla, R.I.3    Wilson, J.M.4
  • 14
    • 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(1):91-6
    • (1998) FEMS Microbiol Lett , vol.160 , Issue.1 , pp. 91-96
    • Subbalakshmi, C.1    Sitaram, N.2
  • 15
    • 0037204044 scopus 로고    scopus 로고
    • Correlation of the antibacterial activities of cationic peptide antibiotics and cationic steroid antibiotics
    • Ding B, Guan Q, Walsh JP et al. Correlation of the antibacterial activities of cationic peptide antibiotics and cationic steroid antibiotics. J Med Chem, 2002;45(3):663-9
    • (2002) J Med Chem , vol.45 , Issue.3 , pp. 663-669
    • Ding, B.1    Guan, Q.2    Walsh, J.P.3
  • 16
    • 0035007963 scopus 로고    scopus 로고
    • Interaction of CAP18-derived peptides with membranes made from endotoxins or phospholipids
    • Gutsmann T, Hagge SO, Larrick O et al. Interaction of CAP18-derived peptides with membranes made from endotoxins or phospholipids. Biophys J, 2001;(80):2935-45
    • (2001) Biophys J , Issue.80 , pp. 2935-2945
    • Gutsmann, T.1    Hagge, S.O.2    Larrick, O.3
  • 17
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses
    • Scott MG, Davidson DJ, Gold MR et al. The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J Immunol, 2002;169(7):3883-91
    • (2002) J Immunol , vol.169 , Issue.7 , pp. 3883-3891
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3
  • 18
    • 0034488452 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides and their multifunctional role in the immune system
    • Scott MG, Hancock RE. Cationic antimicrobial peptides and their multifunctional role in the immune system. Crit Rem Immunol, 2000;20(5):407-31
    • (2000) Crit Rem Immunol , vol.20 , Issue.5 , pp. 407-431
    • Scott, M.G.1    Hancock, R.E.2
  • 19
    • 0035984783 scopus 로고    scopus 로고
    • Potential therapeutic role of cationic peptides in three experimental models of septic shock
    • Giacometti A, Cirioni O, Ghiselli R et al. Potential therapeutic role of cationic peptides in three experimental models of septic shock. Antimicrobial Agents and Chemotherapy, 2002;46(7): 2132-6
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.7 , pp. 2132-2136
    • Giacometti, A.1    Cirioni, O.2    Ghiselli, R.3
  • 20
    • 0344624861 scopus 로고    scopus 로고
    • Dermaseptin, a peptide antibiotic, stimulates microbicidal activities of polymorphonuclear leukocytes
    • Ammar B, Perianin A, Mor A et al. Dermaseptin, a peptide antibiotic, stimulates microbicidal activities of polymorphonuclear leukocytes. Biochem Biophys Res Commun, 1998;247(3):870 -5
    • (1998) Biochem Biophys Res Commun , vol.247 , Issue.3 , pp. 870-875
    • Ammar, B.1    Perianin, A.2    Mor, A.3
  • 21
    • 0036789872 scopus 로고    scopus 로고
    • Antiviral and antitumor peptides from insects
    • Chernysh S, Kim SI, Bekker G et al. Antiviral and antitumor peptides from insects. Proc Natl Acad Sci USA, 2002;99(20): 12628-32
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.20 , pp. 12628-12632
    • Chernysh, S.1    Kim, S.I.2    Bekker, G.3
  • 22
    • 0033737068 scopus 로고    scopus 로고
    • Comparative activities of polycationic peptides and clinically used antimicrobial agents against multidrug-resistant nosocomial isolates of Acineto-bacter baumannii
    • Giacometti A, Cirioni O, Del Prete MS et al. Comparative activities of polycationic peptides and clinically used antimicrobial agents against multidrug-resistant nosocomial isolates of Acineto-bacter baumannii. J Antimicrob Chemother, 2000;46(5):807-10
    • (2000) J Antimicrob Chemother , vol.46 , Issue.5 , pp. 807-810
    • Giacometti, A.1    Cirioni, O.2    Del Prete, M.S.3
  • 23
    • 0033915249 scopus 로고    scopus 로고
    • Characterization of a fish antimicrobial peptide: Gene expression, subcellular localization, and spectrum of activity
    • Cole AM, Darouiche RO, Legarda D et al. Characterization of a fish antimicrobial peptide: Gene expression, subcellular localization, and spectrum of activity. Antimicrobial Agents and Chemotherapy, 2000;44(8):2039-45
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.8 , pp. 2039-2045
    • Cole, A.M.1    Darouiche, R.O.2    Legarda, D.3
  • 24
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan H, Hancock REW. Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrobial Agents and Chemotherapy, 2001;145(5):558-1560
    • (2001) Antimicrobial Agents and Chemotherapy , vol.145 , Issue.5 , pp. 558-1560
    • Yan, H.1    Hancock, R.E.W.2
  • 25
    • 0035038578 scopus 로고    scopus 로고
    • Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin
    • Patrzykat A, Zhang L, Mendoza V et al. Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin. Antimicrob Agents Chemother, 2001;45(5):1337-42
    • (2001) Antimicrob Agents Chemother , vol.45 , Issue.5 , pp. 1337-1342
    • Patrzykat, A.1    Zhang, L.2    Mendoza, V.3
  • 26
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of gram-negative bacteria
    • Matsuzaki K, Sugishita K, Harada M et al. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of gram-negative bacteria. Biochim Biophys Acta, 1997; 1327(1):119-30
    • (1997) Biochim Biophys Acta , vol.1327 , Issue.1 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3
  • 27
    • 0037183527 scopus 로고    scopus 로고
    • Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity
    • Tachi T, Epand RF, Epand RM, Matsuzaki K. Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity. Biochemistry, 2002;41(34):10723-31
    • (2002) Biochemistry , vol.41 , Issue.34 , pp. 10723-10731
    • Tachi, T.1    Epand, R.F.2    Epand, R.M.3    Matsuzaki, K.4
  • 28
    • 0035968224 scopus 로고    scopus 로고
    • Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria
    • Friedrich CL, Rozek A, Patrzykat A, Hancock RE. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria. J Biol Chem, 2001;276(26):24015-22
    • (2001) J Biol Chem , vol.276 , Issue.26 , pp. 24015-24022
    • Friedrich, C.L.1    Rozek, A.2    Patrzykat, A.3    Hancock, R.E.4
  • 29
    • 0034777258 scopus 로고    scopus 로고
    • Structure-function relationships in the tryptophan-rich, antimicrobial peptide indolicidin
    • Staubitz P, Peschel A, Nieuwenhuizen WF et al. Structure-function relationships in the tryptophan-rich, antimicrobial peptide indolicidin. J Pept Sci, 2001;7(10):552-64
    • (2001) J Pept Sci , vol.7 , Issue.10 , pp. 552-564
    • Staubitz, P.1    Peschel, A.2    Nieuwenhuizen, W.F.3
  • 30
    • 0030583546 scopus 로고    scopus 로고
    • Requirements for antibacterial and hemolytic activities in the bovine neutrophil derived 13-residue peptide indolicidin
    • Subbalakshmi C, Krishnakumari V, Nagaraj R, Sitaram N. Requirements for antibacterial and hemolytic activities in the bovine neutrophil derived 13-residue peptide indolicidin. FEBS Lett, 1996;395(1):48-52
    • (1996) FEBS Lett , vol.395 , Issue.1 , pp. 48-52
    • Subbalakshmi, C.1    Krishnakumari, V.2    Nagaraj, R.3    Sitaram, N.4
  • 31
    • 0033485640 scopus 로고    scopus 로고
    • Structural and functional implications of a proline residue in the antimicrobial peptide gaegurin
    • Suh JY, Lee YT, Park CB et al. Structural and functional implications of a proline residue in the antimicrobial peptide gaegurin. Eur J Biochem, 1999;266(2):665-74
    • (1999) Eur J Biochem , vol.266 , Issue.2 , pp. 665-674
    • Suh, J.Y.1    Lee, Y.T.2    Park, C.B.3
  • 32
    • 0037113127 scopus 로고    scopus 로고
    • Role of proline, cysteine, and disulfide bridge in the structure and activity of the antimicrobial peptide gaegurin 5
    • epub ahead of print
    • Park SH, Kim HE, Kim CM et al. Role of proline, cysteine, and disulfide bridge in the structure and activity of the antimicrobial peptide gaegurin 5. Biochem J, 2002;Pt[epub ahead of print]
    • (2002) Biochem J , Issue.PART
    • Park, S.H.1    Kim, H.E.2    Kim, C.M.3
  • 33
    • 0035187785 scopus 로고    scopus 로고
    • Structure-function studies on the amphibian peptide brevinin 1E: Translocating the cationic segment from the C-terminal end to a central position favors selective antibacterial activity
    • Kumari VK, Nagaraj R. Structure-function studies on the amphibian peptide brevinin 1E: Translocating the cationic segment from the C-terminal end to a central position favors selective antibacterial activity. J Pept Res, 2001;58(5):433-41
    • (2001) J Pept Res , vol.58 , Issue.5 , pp. 433-441
    • Kumari, V.K.1    Nagaraj, R.2
  • 34
    • 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(21):5589-600
    • (2001) Eur J Biochem , vol.268 , Issue.21 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 35
    • 0034943549 scopus 로고    scopus 로고
    • A simple method for the purification of an antimicrobial peptide in recombinant Escherichia coli
    • Hwang SW, Lee JH, Park HB et al. A simple method for the purification of an antimicrobial peptide in recombinant Escherichia coli. Mol Biotechnol, 2001;18(3):193-8
    • (2001) Mol Biotechnol , vol.18 , Issue.3 , pp. 193-198
    • Hwang, S.W.1    Lee, J.H.2    Park, H.B.3
  • 36
    • 0034597709 scopus 로고    scopus 로고
    • High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies
    • Lee JH, Kim JH, Hwang SW et al. High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies. Biochem Biophys Res Commun, 2000;277(3):575-80
    • (2000) Biochem Biophys Res Commun , vol.277 , Issue.3 , pp. 575-580
    • Lee, J.H.1    Kim, J.H.2    Hwang, S.W.3
  • 37
    • 0032006495 scopus 로고    scopus 로고
    • Acidic peptide-mediated expression of the antimicrobial peptide buforin II as tandem repeats in escherichia coli
    • Lee JH, Minn I, Park CB, Kim SC. Acidic peptide-mediated expression of the antimicrobial peptide buforin II as tandem repeats in escherichia coli. Protein Expr Purif, 1998;12(1):53 -60
    • (1998) Protein Expr Purif , vol.12 , Issue.1 , pp. 53-60
    • Lee, J.H.1    Minn, I.2    Park, C.B.3    Kim, S.C.4
  • 38
    • 0036135697 scopus 로고    scopus 로고
    • Cathelicidins: A family of endogenous antimicrobial peptides
    • Lehrer RI, Ganz T. Cathelicidins: A family of endogenous antimicrobial peptides. Curr Opin Hematol, 2002;9(1):18-22
    • (2002) Curr Opin Hematol , vol.9 , Issue.1 , pp. 18-22
    • Lehrer, R.I.1    Ganz, T.2
  • 39
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner J, Cho Y, Dinh NN et al. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob Agents Chemother, 1998;42(9):2206-14
    • (1998) Antimicrob Agents Chemother , vol.42 , Issue.9 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3
  • 40
    • 0037057645 scopus 로고    scopus 로고
    • Endogenous antimicrobial peptides and skin infectons in atopic dermatitis
    • Ong PY, Ohtake T, Brandt C et al. Endogenous antimicrobial peptides and skin infectons in atopic dermatitis. N Engl J Med, 2002;347(15):1151-60
    • (2002) N Engl J Med , vol.347 , Issue.15 , pp. 1151-1160
    • Ong, P.Y.1    Ohtake, T.2    Brandt, C.3
  • 41
    • 0032803143 scopus 로고    scopus 로고
    • Reduced antimicrobial peptide expression in human burn wounds
    • Milner SM, Ortega MR. Reduced antimicrobial peptide expression in human burn wounds. Burns, 1999;25(5):411-3
    • (1999) Burns , vol.25 , Issue.5 , pp. 411-413
    • Milner, S.M.1    Ortega, M.R.2
  • 42
    • 0036740432 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 is expressed by keratinocytes in condyloma acuminatum and verruca vulgaris
    • Conner K, Nern K, Rudisill J et al. The antimicrobial peptide LL-37 is expressed by keratinocytes in condyloma acuminatum and verruca vulgaris. J Am Acad Dermatol 2002;47(3):347-50
    • (2002) J Am Acad Dermatol , vol.47 , Issue.3 , pp. 347-350
    • Conner, K.1    Nern, K.2    Rudisill, J.3
  • 43
    • 0036267390 scopus 로고    scopus 로고
    • mig-14 is a salmonella gene that plays a role in bacterial resistance to antimicrobial peptides
    • Brodsky IE, Ernst RK, Miller SI, Falkow S. mig-14 is a salmonella gene that plays a role in bacterial resistance to antimicrobial peptides. J Bacteriol, 2002;184(12):3203-13
    • (2002) J Bacteriol , vol.184 , Issue.12 , pp. 3203-3213
    • Brodsky, I.E.1    Ernst, R.K.2    Miller, S.I.3    Falkow, S.4
  • 44
    • 0035106913 scopus 로고    scopus 로고
    • Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules
    • Bals R, Lang C, Weiner DJ et al. Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules. Clin Diagn Lab Immunol, 2001;8(2):370-5
    • (2001) Clin Diagn Lab Immunol , vol.8 , Issue.2 , pp. 370-375
    • Bals, R.1    Lang, C.2    Weiner, D.J.3


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