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Volumn 26, Issue 12, 2005, Pages 2377-2383

Effects of the terminal charges in human neutrophil α-defensin 2 on its bactericidal and membrane activity

Author keywords

Acetylation; Amidation; Defensin; HNP; Large unilamellar vesicle; Liposome

Indexed keywords

ALPHA DEFENSIN; PEPTIDE DERIVATIVE;

EID: 27944493960     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2005.06.002     Document Type: Article
Times cited : (20)

References (45)
  • 2
    • 0032738473 scopus 로고    scopus 로고
    • Lipid-induced conformation and lipid-binding properties of cytolytic and antimicrobial peptides: Determination and biological specificity
    • S.E. Blondelle, K. Lohner, and M. Aguilar Lipid-induced conformation and lipid-binding properties of cytolytic and antimicrobial peptides: determination and biological specificity Biochim Biophys Acta 1462 1999 89 108
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 89-108
    • Blondelle, S.E.1    Lohner, K.2    Aguilar, M.3
  • 3
    • 10044251130 scopus 로고    scopus 로고
    • Defensins: Natural anti-HIV peptides
    • T.L. Chang, and M.E. Klotman Defensins: natural anti-HIV peptides AIDS Rev 6 2004 161 168
    • (2004) AIDS Rev , vol.6 , pp. 161-168
    • Chang, T.L.1    Klotman, M.E.2
  • 4
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of {alpha}-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Y. Chen, C.T. Mant, S.W. Farmer, R.E. Hancock, M.L. Vasil, and R.S. Hodges Rational design of {alpha}-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index J Biol Chem 280 2005 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
  • 5
    • 0021890825 scopus 로고
    • 2+-induced fusion and destabilization of liposomes
    • 2+-induced fusion and destabilization of liposomes Biochemistry 24 1985 3099 3106
    • (1985) Biochemistry , vol.24 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 6
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • R.M. Epand, and H.J. Vogel Diversity of antimicrobial peptides and their mechanisms of action Biochim Biophys Acta 1462 1999 11 28
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 7
    • 11244342346 scopus 로고    scopus 로고
    • Antibacterial activity and specificity of the six human {alpha}-defensins
    • B. Ericksen, Z. Wu, W. Lu, and R.I. Lehrer Antibacterial activity and specificity of the six human {alpha}-defensins Antimicrob Agents Chemother 49 2005 269 275
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 269-275
    • Ericksen, B.1    Wu, Z.2    Lu, W.3    Lehrer, R.I.4
  • 8
    • 4644322849 scopus 로고    scopus 로고
    • Bacterial evasion of innate host defenses - The Staphylococcus aureus lesson
    • I. Fedtke, F. Gotz, and A. Peschel Bacterial evasion of innate host defenses - the Staphylococcus aureus lesson Int J Med Microbiol 294 2004 189 194
    • (2004) Int J Med Microbiol , vol.294 , pp. 189-194
    • Fedtke, I.1    Gotz, F.2    Peschel, A.3
  • 9
    • 0033915369 scopus 로고    scopus 로고
    • Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria
    • C.L. Friedrich, D. Moyles, T.J. Beveridge, and R.E. Hancock Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria Antimicrob Agents Chemother 44 2000 2086 2092
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 2086-2092
    • Friedrich, C.L.1    Moyles, D.2    Beveridge, T.J.3    Hancock, R.E.4
  • 10
    • 0027218376 scopus 로고
    • Defensins promote fusion and lysis of negatively charged membranes
    • G. Fujii, M.E. Selsted, and D. Eisenberg Defensins promote fusion and lysis of negatively charged membranes Protein Sci 2 1993 1301 1312
    • (1993) Protein Sci , vol.2 , pp. 1301-1312
    • Fujii, G.1    Selsted, M.E.2    Eisenberg, D.3
  • 11
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • T. Ganz Defensins: antimicrobial peptides of innate immunity Nat Immunol 3 2003 710 720
    • (2003) Nat Immunol , vol.3 , pp. 710-720
    • Ganz, T.1
  • 12
    • 1642284891 scopus 로고    scopus 로고
    • Bactericidal cationic peptides can also function as bacteriolysis- inducing agents mimicking beta-lactam antibiotics?; It is enigmatic why this concept is consistently disregarded
    • I. Ginsburg Bactericidal cationic peptides can also function as bacteriolysis-inducing agents mimicking beta-lactam antibiotics?; it is enigmatic why this concept is consistently disregarded Med Hypotheses 62 2004 367 374
    • (2004) Med Hypotheses , vol.62 , pp. 367-374
    • Ginsburg, I.1
  • 13
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • R.E. Hancock Peptide antibiotics Lancet 349 1997 418 422
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.1
  • 14
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • R.E. Hancock, and R. Lehrer Cationic peptides: a new source of antibiotics Trends Biotechnol 16 1998 82 88
    • (1998) Trends Biotechnol , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 15
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • R.E. Hancock, and A. Rozek Role of membranes in the activities of antimicrobial cationic peptides FEMS Microbiol Lett 206 2002 143 149
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 143-149
    • Hancock, R.E.1    Rozek, A.2
  • 16
    • 0030827974 scopus 로고    scopus 로고
    • Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins
    • K. Hristova, M.E. Selsted, and S.H. White Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins J Biol Chem 272 1997 24224 24233
    • (1997) J Biol Chem , vol.272 , pp. 24224-24233
    • Hristova, K.1    Selsted, M.E.2    White, S.H.3
  • 17
    • 0013621551 scopus 로고
    • Structure-function studies of peptide hormones: An overview
    • B. Gutte Academic Press San Diego
    • V.J. Hruby, and D. Patel Structure-function studies of peptide hormones: an overview B. Gutte Peptides: synthesis, structures, and applications 1995 Academic Press San Diego
    • (1995) Peptides: Synthesis, Structures, and Applications
    • Hruby, V.J.1    Patel, D.2
  • 18
    • 0033532175 scopus 로고    scopus 로고
    • Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity
    • L.H. Kondejewski, M. Jelokhani-Niaraki, S.W. Farmer, B. Lix, C.M. Kay, and B.D. Sykes Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity J Biol Chem 274 1999 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
  • 19
    • 4444246692 scopus 로고    scopus 로고
    • Primate defensins
    • R.I. Lehrer Primate defensins Nat Rev Microbiol 2 2004 727 738
    • (2004) Nat Rev Microbiol , vol.2 , pp. 727-738
    • Lehrer, R.I.1
  • 21
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • K. Matsuzaki Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes Biochim Biophys Acta 1462 1999 1 10
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 23
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • C.N. Pace, F. Vajdos, L. Fee, G. Grimsley, and T. Gray How to measure and predict the molar absorption coefficient of a protein Protein Sci 4 1995 2411 2423
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 24
    • 0034194257 scopus 로고    scopus 로고
    • Large-scale synthesis and functional elements for the antimicrobial activity of defensins
    • P.A. Raj, K.J. Antonyraj, and T. Karunakaran Large-scale synthesis and functional elements for the antimicrobial activity of defensins Biochem J 347 Pt 3 2000 633 641
    • (2000) Biochem J , vol.347 , Issue.3 PART , pp. 633-641
    • Raj, P.A.1    Antonyraj, K.J.2    Karunakaran, T.3
  • 26
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • M. Schnolzer, P. Alewood, A. Jones, D. Alewood, and S.B. Kent In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences Int J Pept Protein Res 40 1992 180 193
    • (1992) Int J Pept Protein Res , vol.40 , pp. 180-193
    • Schnolzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 28
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim Biophys Acta 1462 1999 55 70
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 29
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Y. Shai Mode of action of membrane active antimicrobial peptides Biopolymers 66 2002 236 248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 30
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity
    • N. Sitaram, and R. Nagaraj Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity Biochim Biophys Acta 1462 1999 29 54
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 31
    • 12144289841 scopus 로고    scopus 로고
    • Structure-activity determinants in paneth cell alpha-defensins: Loss-of-function in mouse cryptdin-4 by charge-reversal at arginine residue positions
    • H. Tanabe, X. Qu, C.S. Weeks, J.E. Cummings, S. Kolusheva, and K.B. Walsh Structure-activity determinants in paneth cell alpha-defensins: loss-of-function in mouse cryptdin-4 by charge-reversal at arginine residue positions J Biol Chem 279 2004 11976 11983
    • (2004) J Biol Chem , vol.279 , pp. 11976-11983
    • Tanabe, H.1    Qu, X.2    Weeks, C.S.3    Cummings, J.E.4    Kolusheva, S.5    Walsh, K.B.6
  • 33
    • 0037407586 scopus 로고    scopus 로고
    • Retrocyclin, an antiretroviral theta-defensin, is a lectin
    • W. Wang, A.M. Cole, T. Hong, A.J. Waring, and R.I. Lehrer Retrocyclin, an antiretroviral theta-defensin, is a lectin J Immunol 170 2003 4708 4716
    • (2003) J Immunol , vol.170 , pp. 4708-4716
    • Wang, W.1    Cole, A.M.2    Hong, T.3    Waring, A.J.4    Lehrer, R.I.5
  • 34
    • 2942729771 scopus 로고    scopus 로고
    • Activity of alpha- and theta-defensins against primary isolates of HIV-1
    • W. Wang, S.M. Owen, D.L. Rudolph, A.M. Cole, T. Hong, and A.J. Waring Activity of alpha- and theta-defensins against primary isolates of HIV-1 J Immunol 173 2004 515 520
    • (2004) J Immunol , vol.173 , pp. 515-520
    • Wang, W.1    Owen, S.M.2    Rudolph, D.L.3    Cole, A.M.4    Hong, T.5    Waring, A.J.6
  • 35
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • W.C. Wimley, M.E. Selsted, and S.H. White Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores Protein Sci 3 1994 1362 1373
    • (1994) Protein Sci , vol.3 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 36
    • 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
    • M. Wu, E. Maier, R. Benz, and R.E. Hancock Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli Biochemistry 38 1999 7235 7242
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.4
  • 37
  • 38
    • 0042808526 scopus 로고    scopus 로고
    • Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human β-defensin 3
    • Z. Wu, D.M. Hoover, D. Yang, C. Boulegue, F. Santamaria, and J. Oppenheim Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human β-defensin 3 Proc Natl Acad Sci USA 100 2003 8880 8885
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8880-8885
    • Wu, Z.1    Hoover, D.M.2    Yang, D.3    Boulegue, C.4    Santamaria, F.5    Oppenheim, J.6
  • 39
    • 0037420319 scopus 로고    scopus 로고
    • Productive folding of human neutrophil α-defensins in vitro without the pro-peptide
    • Z. Wu, R. Powell, and W. Lu Productive folding of human neutrophil α-defensins in vitro without the pro-peptide J Am Chem Soc 125 2003 2402 2403
    • (2003) J Am Chem Soc , vol.125 , pp. 2402-2403
    • Wu, Z.1    Powell, R.2    Lu, W.3
  • 40
    • 0038345623 scopus 로고    scopus 로고
    • From pro defensins to defensins: Synthesis and characterization of human neutrophil pro a-defensin-1 and its mature domain
    • Z. Wu, A. Prahl, R. Powell, B. Ericksen, J. Lubkowski, and W. Lu From pro defensins to defensins: synthesis and characterization of human neutrophil pro a-defensin-1 and its mature domain J Pept Res 62 2003 53 62
    • (2003) J Pept Res , vol.62 , pp. 53-62
    • Wu, Z.1    Prahl, A.2    Powell, R.3    Ericksen, B.4    Lubkowski, J.5    Lu, W.6
  • 41
    • 25444478690 scopus 로고    scopus 로고
    • Reconstruction of the conserved beta-bulge in mammalian defensins using d-amino acids
    • C. Xie, A. Prahl, B. Ericksen, Z. Wu, P. Zeng, and X. Li Reconstruction of the conserved beta-bulge in mammalian defensins using d-amino acids J Biol Chem 2005
    • (2005) J Biol Chem
    • Xie, C.1    Prahl, A.2    Ericksen, B.3    Wu, Z.4    Zeng, P.5    Li, X.6
  • 42
    • 0033844287 scopus 로고    scopus 로고
    • Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells
    • D. Yang, Q. Chen, O. Chertov, and J.J. Oppenheim Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells J Leukoc Biol 68 2000 9 14
    • (2000) J Leukoc Biol , vol.68 , pp. 9-14
    • Yang, D.1    Chen, Q.2    Chertov, O.3    Oppenheim, J.J.4
  • 43
    • 0033569408 scopus 로고    scopus 로고
    • Beta-defensins: Linking innate and adaptive immunity through dendritic and T cell CCR6
    • D. Yang, O. Chertov, S.N. Bykovskaia, Q. Chen, M.J. Buffo, and J. Shogan Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6 Science 286 1999 525 528
    • (1999) Science , vol.286 , pp. 525-528
    • Yang, D.1    Chertov, O.2    Bykovskaia, S.N.3    Chen, Q.4    Buffo, M.J.5    Shogan, J.6
  • 44
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 45
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • L. Zhang, A. Rozek, and R.E. Hancock Interaction of cationic antimicrobial peptides with model membranes J Biol Chem 276 2001 35714 35722
    • (2001) J Biol Chem , vol.276 , pp. 35714-35722
    • Zhang, L.1    Rozek, A.2    Hancock, R.E.3


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