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Volumn 239, Issue 2, 2004, Pages 295-299

Factors contributing to the potency of antimicrobial cationic peptides from the N-terminal region of human lactoferrin

Author keywords

Cationic antimicrobial peptides; Human lactoferrin peptide; Lactoferrin

Indexed keywords

ANTIINFECTIVE AGENT; GLYCINE; LACTOFERRIN; PEPTIDE DERIVATIVE; TRYPTOPHAN;

EID: 5144230602     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2004.08.048     Document Type: Article
Times cited : (5)

References (32)
  • 1
    • 0036191387 scopus 로고    scopus 로고
    • The physiology of lactoferrin
    • J.H. Brock The physiology of lactoferrin Biochem. Cell Biol. 80 2002 1 6
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 1-6
    • Brock, J.H.1
  • 2
    • 0141918811 scopus 로고    scopus 로고
    • Lactoferrin - A multifunctional protein with antimicrobial properties
    • S. Farnaud, and R.W. Evans Lactoferrin - a multifunctional protein with antimicrobial properties Mol. Immunol. 40 2003 395 405
    • (2003) Mol. Immunol. , vol.40 , pp. 395-405
    • Farnaud, S.1    Evans, R.W.2
  • 3
    • 0014428034 scopus 로고
    • Inhibition of bacteria by lactoferrin and other iron-chelating agents
    • J.D. Oram, and B. Reiter Inhibition of bacteria by lactoferrin and other iron-chelating agents Biochim. Biophys. Acta 170 1968 351 365
    • (1968) Biochim. Biophys. Acta , vol.170 , pp. 351-365
    • Oram, J.D.1    Reiter, B.2
  • 4
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • R.R. Arnold, R.M. Cole, and J.R. McGhee A bactericidal effect for human lactoferrin Science 197 1977 263 265
    • (1977) Science , vol.197 , pp. 263-265
    • Arnold, R.R.1    Cole, R.M.2    McGhee, J.R.3
  • 5
    • 0015023117 scopus 로고
    • The bacteriostatic effect of serum on Pasteurella septica and its abolition by iron compounds
    • J.J. Bullen, H.J. Rogers, and J.E. Lewin The bacteriostatic effect of serum on Pasteurella septica and its abolition by iron compounds Immunology 20 1971 391 406
    • (1971) Immunology , vol.20 , pp. 391-406
    • Bullen, J.J.1    Rogers, H.J.2    Lewin, J.E.3
  • 6
    • 0022643302 scopus 로고
    • Bactericidal effect of lactoferrin on Legionella pneumophila
    • C.A. Bortner, R.D. Miller, and R.R. Arnold Bactericidal effect of lactoferrin on Legionella pneumophila Infect. Immun. 51 1986 373 377
    • (1986) Infect. Immun. , vol.51 , pp. 373-377
    • Bortner, C.A.1    Miller, R.D.2    Arnold, R.R.3
  • 7
    • 0023736956 scopus 로고
    • Killing of Actinobacillus actinomycetemcomitans by human lactoferrin
    • J.R. Kalmer, and R.R. Arnold Killing of Actinobacillus actinomycetemcomitans by human lactoferrin Infect. Immun. 56 1988 2552 2557
    • (1988) Infect. Immun. , vol.56 , pp. 2552-2557
    • Kalmer, J.R.1    Arnold, R.R.2
  • 8
    • 0026095436 scopus 로고
    • Killing of Gram-negative bacteria by lactoferrin and lysozyme
    • R.T. Ellison III, and T.J. Giehl Killing of Gram-negative bacteria by lactoferrin and lysozyme J. Clin. Inv. 88 1991 1080 1091
    • (1991) J. Clin. Inv. , vol.88 , pp. 1080-1091
    • Ellison III, R.T.1    Giehl, T.J.2
  • 11
    • 0029930976 scopus 로고    scopus 로고
    • Antibacterial activity of peptides homologous to a loop region in human lactoferrin
    • E.W. Odell, R. Sarra, M. Foxworthy, D.S. Chapple, and R.W. Evans Antibacterial activity of peptides homologous to a loop region in human lactoferrin FEBS Lett. 382 1996 175 178
    • (1996) FEBS Lett. , vol.382 , pp. 175-178
    • Odell, E.W.1    Sarra, R.2    Foxworthy, M.3    Chapple, D.S.4    Evans, R.W.5
  • 12
    • 0029860472 scopus 로고    scopus 로고
    • Structure-biological activity relationship of 11-residue highly basic peptide segment of bovine lactoferrin
    • J.H. Kang, M.K. Lee, K.L. Kim, and K.S. Hahan Structure-biological activity relationship of 11-residue highly basic peptide segment of bovine lactoferrin Int. J. Prot. Res. 48 1996 357 363
    • (1996) Int. J. Prot. Res. , vol.48 , pp. 357-363
    • Kang, J.H.1    Lee, M.K.2    Kim, K.L.3    Hahan, K.S.4
  • 13
    • 0031839843 scopus 로고    scopus 로고
    • Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin
    • D.S. Chapple, D.J. Mason, C.L. Joannou, E.W. Odell, V. Gant, and R.W. Evans Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin Infect. Immun. 66 1998 2434 2440
    • (1998) Infect. Immun. , vol.66 , pp. 2434-2440
    • Chapple, D.S.1    Mason, D.J.2    Joannou, C.L.3    Odell, E.W.4    Gant, V.5    Evans, R.W.6
  • 15
    • 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
  • 17
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • A. Tossi, L. Sandri, and A. Giangaspero Amphipathic, alpha-helical antimicrobial peptides Biopolymers 55 2000 4 30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 18
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic α helical antimicrobial peptides
    • A. Giangaspero, L. Sandri, and A. Tossi Amphipathic α helical antimicrobial peptides Europ. J. Biochem. 268 2001 5589 5600
    • (2001) Europ. J. Biochem. , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 19
    • 0035014876 scopus 로고    scopus 로고
    • The role of tryptophan in the antibacterial activity of a 15-residue bovine lactoferricin peptide
    • B.E. Haug, and J.S. Svendsen The role of tryptophan in the antibacterial activity of a 15-residue bovine lactoferricin peptide J. Peptide Sci. 7 2001 190 196
    • (2001) J. Peptide Sci. , vol.7 , pp. 190-196
    • Haug, B.E.1    Svendsen, J.S.2
  • 20
    • 0036185339 scopus 로고    scopus 로고
    • Towards structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides
    • H.J. Vogel, D.J. Schibli, W. Jing, E.M. Lohmeier-Vogel, R.F. Epand, and R.M. Epand Towards structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides Biochem. Cell Biol. 80 2002 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
  • 21
    • 0346034649 scopus 로고    scopus 로고
    • Tryptophan-rich antimicrobial peptides: Comparative properties and membrane interactions
    • D.J. Schibli, R.F. Epand, H.J. Vogel, and R.M. Epand Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions Biochem. Cell Biol. 80 2002 667 677
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 667-677
    • Schibli, D.J.1    Epand, R.F.2    Vogel, H.J.3    Epand, R.M.4
  • 22
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • W.L. Maloy, and U.P. Kari Structure-activity studies on magainins and other host defense peptides Biopolymers 37 1995 105 122
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 23
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: Facets of their conformational features, structure and function correlations and membrane-perturbing abilities
    • G. Saberwal, and R. Nagaraj Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure and function correlations and membrane-perturbing abilities BBA-Rev. Biomembranes 1197 1994 109 131
    • (1994) BBA-Rev. Biomembranes , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nagaraj, R.2
  • 24
    • 0026557830 scopus 로고
    • The functions of tryptophan residues in membrane proteins
    • M. Schiffer, C.H. Chang, and F.J. Stevens The functions of tryptophan residues in membrane proteins Protein Eng. 5 1992 213 214
    • (1992) Protein Eng. , vol.5 , pp. 213-214
    • Schiffer, M.1    Chang, C.H.2    Stevens, F.J.3
  • 25
    • 0029766187 scopus 로고    scopus 로고
    • Folding proteins into membranes
    • C.M. Deber, and N.K. Goto Folding proteins into membranes Nat. Struct. Biol. 3 1996 815 818
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 815-818
    • Deber, C.M.1    Goto, N.K.2
  • 26
    • 0032907969 scopus 로고    scopus 로고
    • Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide
    • M. Wu, and R.E.W. Hancock Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide Antimicrob. Agents Chemother. 43 1999 1274 1276
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1274-1276
    • Wu, M.1    Hancock, R.E.W.2
  • 27
    • 0030586288 scopus 로고    scopus 로고
    • Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides
    • C. Lawyer, S. Pai, M. Watabe, P. Borgia, T. Mashimo, L. Eagleton, and K. Watabe Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides FEBS Lett. 390 1996 95 98
    • (1996) FEBS Lett. , vol.390 , pp. 95-98
    • Lawyer, C.1    Pai, S.2    Watabe, M.3    Borgia, P.4    Mashimo, T.5    Eagleton, L.6    Watabe, K.7
  • 29
    • 0002548661 scopus 로고    scopus 로고
    • Effect of introducing p-fluorophenylalanine and multiple tryptophan residues in a 13-residue antibacterial peptide
    • E. Bikshapathy, N. Sitaram, and R. Nagaraj Effect of introducing p-fluorophenylalanine and multiple tryptophan residues in a 13-residue antibacterial peptide Protein Pept. Lett. 6 1999 67 71
    • (1999) Protein Pept. Lett. , vol.6 , pp. 67-71
    • Bikshapathy, E.1    Sitaram, N.2    Nagaraj, R.3
  • 31
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale of proteins at membrane interfaces
    • W.C. Wimley, and S.H. White Experimentally determined hydrophobicity scale of proteins at membrane interfaces Nat. Struct. Biol. 3 1996 815 818
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 815-818
    • Wimley, W.C.1    White, S.H.2
  • 32
    • 0033787915 scopus 로고    scopus 로고
    • Antibacterial activity of 15-residues lactoferricin derivatives
    • M.B. Strøm, O. Rekdal, and J.S. Svendsen Antibacterial activity of 15-residues lactoferricin derivatives J. Peptide Res. 56 2000 265 274
    • (2000) J. Peptide Res. , vol.56 , pp. 265-274
    • Strøm, M.B.1    Rekdal, O.2    Svendsen, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.