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Volumn 16, Issue 4, 2010, Pages 171-177

Structure-activity relationship of indolicidin, a Trp-rich antibacterial peptide

Author keywords

Antibiotic activity; Antimicrobial peptide; Hemolytic activity; Indolicidin; Retro peptide

Indexed keywords

ARGININE; INDOLICIDIN; INDOLICIDIN DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 77949755883     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1217     Document Type: Article
Times cited : (41)

References (36)
  • 1
    • 0029971979 scopus 로고    scopus 로고
    • Peptide antibiotics: Holy or heretic grails of innate immunity?
    • Boman HG. Peptide antibiotics: holy or heretic grails of innate immunity? Scand. J. Immunol. 1996; 43: 475-482.
    • (1996) Scand. J. Immunol , vol.43 , pp. 475-482
    • Boman, H.G.1
  • 2
    • 0032005344 scopus 로고    scopus 로고
    • Antimicrobial peptides of vertebrates
    • Ganz T, Lehrer RI. Antimicrobial peptides of vertebrates. Curr. Opin. Immunol. 1998; 10: 41-44.
    • (1998) Curr. Opin. Immunol , vol.10 , pp. 41-44
    • Ganz, T.1    Lehrer, R.I.2
  • 3
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: Facets of their conformational features, structure-function correlations and membrane perturbing activities
    • Saberwal G, Nagaraj R. Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane perturbing activities. Biochim. Biophys. Acta 1994; 1197: 109-131.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nagaraj, R.2
  • 4
    • 0033864862 scopus 로고    scopus 로고
    • Tossi A, Sandri L, Giangaspero A. Amphipathic, α-helical antimicrobial peptides. Biopolymers 2000; 55: 4-30.
    • Tossi A, Sandri L, Giangaspero A. Amphipathic, α-helical antimicrobial peptides. Biopolymers 2000; 55: 4-30.
  • 5
    • 0029153215 scopus 로고
    • Peptides in membranes: Helicity and hydrophobicity
    • Deber CM, Li S-C. Peptides in membranes: helicity and hydrophobicity. Biopolymers 1995; 37: 295-318.
    • (1995) Biopolymers , vol.37 , pp. 295-318
    • Deber, C.M.1    Li, S.-C.2
  • 6
    • 0034824597 scopus 로고    scopus 로고
    • From 'carpet' mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • Shai Y, Oren Z. From 'carpet' mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides. Peptides 2001; 22: 1629-1641.
    • (2001) Peptides , vol.22 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 7
    • 0036467404 scopus 로고    scopus 로고
    • General aspect of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphiphilic helical model peptides
    • Dathe M, Meyer J, Beyerman M, Maul B, Hoischen C, Bienert M. General aspect of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphiphilic helical model peptides. Biochim. Biophys. Acta 2002; 1558: 171-186.
    • (2002) Biochim. Biophys. Acta , vol.1558 , pp. 171-186
    • Dathe, M.1    Meyer, J.2    Beyerman, M.3    Maul, B.4    Hoischen, C.5    Bienert, M.6
  • 8
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock REW. Peptide antibiotics. Lancet 1997; 349: 418-422.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.W.1
  • 9
    • 2042513493 scopus 로고    scopus 로고
    • 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. U.S.A. 1987; 84: 5449-5453.
    • 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. U.S.A. 1987; 84: 5449-5453.
  • 10
    • 33645820597 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of β-defensins,multi-functional peptides of the immune system
    • Klüver E, Adermann K, Schulz A. Synthesis and structure-activity relationship of β-defensins,multi-functional peptides of the immune system. J. Pept. Sci. 2006; 12: 243-257.
    • (2006) J. Pept. Sci , vol.12 , pp. 243-257
    • Klüver, E.1    Adermann, K.2    Schulz, A.3
  • 11
    • 4143113468 scopus 로고    scopus 로고
    • Structure-activity relationship ofanantibacterialpeptide,maculatin 1.1, from the skin glands of the tree frog, Litoria genimaculata
    • Niidome T, Kobayashi K, Arakawa H, Hatakeyama T, Aoyagi H. Structure-activity relationship ofanantibacterialpeptide,maculatin 1.1, from the skin glands of the tree frog, Litoria genimaculata. J. Pept. Sci. 2004; 10: 414-422.
    • (2004) J. Pept. Sci , vol.10 , pp. 414-422
    • Niidome, T.1    Kobayashi, K.2    Arakawa, H.3    Hatakeyama, T.4    Aoyagi, H.5
  • 13
    • 0026722445 scopus 로고    scopus 로고
    • Selsted ME, Novotny MJ, Morris WL, Tang YQ, Smith W, Cullor JS. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J. Biol. Chem. 1992; 267: 4292-4295.
    • Selsted ME, Novotny MJ, Morris WL, Tang YQ, Smith W, Cullor JS. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J. Biol. Chem. 1992; 267: 4292-4295.
  • 14
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptides of mammalian cells
    • Lehrer RI, Lichtenstein AK, Ganz T. Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 1993; 11: 109-128.
    • (1993) Annu. Rev. Immunol , vol.11 , pp. 109-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 15
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: Facets of their conformational features, structure-function correlations and membrane-perturbing abilities
    • Saberwal G, Nagaraj R. Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities. Biochim. Biophys. Acta 1994; 1197: 109-132.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 109-132
    • Saberwal, G.1    Nagaraj, R.2
  • 16
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman HG. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 1995; 13: 61-62.
    • (1995) Annu. Rev. Immunol , vol.13 , pp. 61-62
    • Boman, H.G.1
  • 17
    • 0027043261 scopus 로고
    • Design of model amphipathic peptides having potent antimicrobial activities
    • Blondelle SE, Houghten RA. Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry 1992; 31: 12688-12694.
    • (1992) Biochemistry , vol.31 , pp. 12688-12694
    • Blondelle, S.E.1    Houghten, R.A.2
  • 18
    • 33645959250 scopus 로고    scopus 로고
    • Design of perfectly symmetric Trp-rich peptides with potent and broad-spectrum antimicrobial activities
    • Yang S-T, Shin SY, Hahm K-S, Kim JI. Design of perfectly symmetric Trp-rich peptides with potent and broad-spectrum antimicrobial activities. Int. J. Antimicrob. Agents 2006; 27: 325-330.
    • (2006) Int. J. Antimicrob. Agents , vol.27 , pp. 325-330
    • Yang, S.-T.1    Shin, S.Y.2    Hahm, K.-S.3    Kim, J.I.4
  • 19
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • Chan DI, Prenner EJ, Vogel HJ. 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
  • 20
    • 33847151791 scopus 로고    scopus 로고
    • Cation-π interactions stabilize the structure of the antimicrobial peptide indolicidin near membranes: Moleculardynamics simulations
    • Khandelia H, Kaznessis YN. Cation-π interactions stabilize the structure of the antimicrobial peptide indolicidin near membranes: moleculardynamics simulations. J.Phys.Chem.B 2007;111:242-250.
    • (2007) J.Phys.Chem.B , vol.111 , pp. 242-250
    • Khandelia, H.1    Kaznessis, Y.N.2
  • 21
    • 33645015808 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action: Studies of Indolicidin assembly at model membrane interfaces by in situ atomic force microscopy
    • Shaw JE, Alattia J-R, Verity JE, Prive GG, Yip CM. Mechanisms of antimicrobial peptide action: studies of Indolicidin assembly at model membrane interfaces by in situ atomic force microscopy. J. Struct. Biol. 2006; 154: 42-58.
    • (2006) J. Struct. Biol , vol.154 , pp. 42-58
    • Shaw, J.E.1    Alattia, J.-R.2    Verity, J.E.3    Prive, G.G.4    Yip, C.M.5
  • 22
    • 0029163069 scopus 로고
    • Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo antifungal activity
    • Ahmad I, Perkins WR, Lupan DM, Selsted ME, Janoff AS. Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo antifungal activity. Biochim. Biophys. Acta 1995; 1237: 109-114.
    • (1995) Biochim. Biophys. Acta , vol.1237 , pp. 109-114
    • Ahmad, I.1    Perkins, W.R.2    Lupan, D.M.3    Selsted, M.E.4    Janoff, A.S.5
  • 26
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • Zhang L,Rozek A,Hancock REW.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.W.3
  • 27
    • 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 REW. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria. J Biol Chem 2001; 276: 24015-24022.
    • (2001) J Biol Chem , vol.276 , pp. 24015-24022
    • Friedrich, C.L.1    Rozek, A.2    Patrzykat, A.3    Hancock, R.E.W.4
  • 28
    • 48249123462 scopus 로고    scopus 로고
    • Bacterial selectivity and plausible mode of antibacterial action of designed Pro-rich short model antimicrobial peptides
    • Park KH, Park Y, Park IS, Hahm KS, Shin SY. Bacterial selectivity and plausible mode of antibacterial action of designed Pro-rich short model antimicrobial peptides. J Pept. Sci. 2008; 14: 876-882.
    • (2008) J Pept. Sci , vol.14 , pp. 876-882
    • Park, K.H.1    Park, Y.2    Park, I.S.3    Hahm, K.S.4    Shin, S.Y.5
  • 30
    • 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: 2158-2167.
    • (2002) Protein Sci , vol.11 , pp. 2158-2167
    • Nagpal, S.1    Kaur, K.J.2    Jain, D.3    Salunke, D.M.4
  • 31
    • 0035134035 scopus 로고    scopus 로고
    • Interaction of pleurocidin and its analogs with phospholipids membrane and their antibacterial activity
    • Yoshida K, Mukai Y, Niidome T, Takashi C, Tokunaga Y, Hatakeyama T, Aoyagi H. Interaction of pleurocidin and its analogs with phospholipids membrane and their antibacterial activity. J. Pept. Res. 2001; 57: 119-126.
    • (2001) J. Pept. Res , vol.57 , pp. 119-126
    • Yoshida, K.1    Mukai, Y.2    Niidome, T.3    Takashi, C.4    Tokunaga, Y.5    Hatakeyama, T.6    Aoyagi, H.7
  • 33
    • 33645837211 scopus 로고    scopus 로고
    • Circular dichroic properties of the tyrosine residues in tetrazole analogues of opioid peptides
    • Lisowski M, Olczak J, Zabrocki J. Circular dichroic properties of the tyrosine residues in tetrazole analogues of opioid peptides. J. Pept. Sci. 2006; 12: 297-302.
    • (2006) J. Pept. Sci , vol.12 , pp. 297-302
    • Lisowski, M.1    Olczak, J.2    Zabrocki, J.3
  • 34
    • 0033592458 scopus 로고    scopus 로고
    • CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix
    • Ladokhin AS, Selsted ME, White SH. CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix. Biochemistry 1999; 38: 12313-12319.
    • (1999) Biochemistry , vol.38 , pp. 12313-12319
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 35
    • 33749076672 scopus 로고    scopus 로고
    • Solvent-dependent structure of two tryptophan-rich antimicrobial peptides and their analogs studied by FTIR and CD specrtoscopy
    • Andrushchenko VV, Vogel HJ, Prenner EJ. Solvent-dependent structure of two tryptophan-rich antimicrobial peptides and their analogs studied by FTIR and CD specrtoscopy. Biochim. Biophys. Acta 2006; 1758: 1596-1608.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1596-1608
    • Andrushchenko, V.V.1    Vogel, H.J.2    Prenner, E.J.3
  • 36
    • 0027447199 scopus 로고
    • Antimicrobial specificity and hemolytic activity of cyclized basic amphiphilic β-structuralmodelpeptidesandtheir interactionswithphospholipid bilayers
    • Ando S, Nishikawa H, Takiguchi H, Lee S, Sugihara G. Antimicrobial specificity and hemolytic activity of cyclized basic amphiphilic β-structuralmodelpeptidesandtheir interactionswithphospholipid bilayers. Biochim. Biophys. Acta 1993; 1147: 42-49.
    • (1993) Biochim. Biophys. Acta , vol.1147 , pp. 42-49
    • Ando, S.1    Nishikawa, H.2    Takiguchi, H.3    Lee, S.4    Sugihara, G.5


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