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Volumn 15, Issue 9, 2009, Pages 569-575

Cell selectivity and mechanism of action of short antimicrobial peptides designed from the cell-penetrating peptide Pep-1

Author keywords

Antimicrobial peptide; Cell selectivity; Cell penetrating peptide; Mechanism of action; Pep 1; Pep 1 K

Indexed keywords

CALCEIN; INDOLICIDIN; LYSYLLYSYLPROLYLTRYPTOPHANYLTRYPTOPHANYLLYSYLPROLYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTRYPTOPHANYLLYSYLLYSYL; LYSYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTRYPTOPHANYL; LYSYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTRYPTOPHANYLLYSYLLYSYL; LYSYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTRYPTOPHANYLSERYLGLUTAMYLPROLYL; LYSYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTRYPTOPHANYLSERYLGLUTAMYLPROLYLLYSYLLYSYL; LYSYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTHREONYLTRYPTOPHANYLTRYPTOPHANYLLYSYLTRYPTOPHANYLSERYLGLUTAMYLPROLYLLYSYLLYSYLLYSYLARGINYLLYSYLVALINYL; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 70349636911     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1145     Document Type: Conference Paper
Times cited : (33)

References (37)
  • 1
    • 3343010545 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of bilogically active proteins into mammalian cells
    • Morris MC, Depollier J, Mery J, Heitz F, Divita G. A peptide carrier for the delivery of bilogically active proteins into mammalian cells. Nat. Biotechnol. 2001; 19: 1143-1147.
    • (2001) Nat. Biotechnol , vol.19 , pp. 1143-1147
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 2
    • 3343017389 scopus 로고    scopus 로고
    • Consequences of nonlytic membrane perturbation to the translocation of the cell penetrating peptide pep-1 in lipidic vesicles
    • Henriques ST, Castanho MARB. Consequences of nonlytic membrane perturbation to the translocation of the cell penetrating peptide pep-1 in lipidic vesicles. Biochemistry 2004; 43: 9716-9724.
    • (2004) Biochemistry , vol.43 , pp. 9716-9724
    • Henriques, S.T.1    Castanho, M.A.R.B.2
  • 3
    • 23044485527 scopus 로고    scopus 로고
    • Translocation of betagalactosidase mediated by the cell-penetrating peptide pep-1 into lipid vesicles and human HeLa cells is driven by membrane electrostatic potential
    • Henriques ST, Costa J, Castanho MA. Translocation of betagalactosidase mediated by the cell-penetrating peptide pep-1 into lipid vesicles and human HeLa cells is driven by membrane electrostatic potential. Biochemistry 2005; 44: 10189-10198.
    • (2005) Biochemistry , vol.44 , pp. 10189-10198
    • Henriques, S.T.1    Costa, J.2    Castanho, M.A.3
  • 5
    • 33749385780 scopus 로고    scopus 로고
    • Cell-penetrating peptides and antimicrobial peptides: How different are they?
    • Henriques ST, Melo MN, Castanho MA. Cell-penetrating peptides and antimicrobial peptides: how different are they? Biochem. J. 2006; 399: 1-7.
    • (2006) Biochem. J , vol.399 , pp. 1-7
    • Henriques, S.T.1    Melo, M.N.2    Castanho, M.A.3
  • 6
    • 33748416305 scopus 로고    scopus 로고
    • Design and mechanism of action of a novel bacteria-selective antimicrobial peptide from the cell-penetrating peptide Pep-1
    • Zhu WL, Lan H, Park IS, Kim JI, Jin HZ, Hahm KS, Shin SY. Design and mechanism of action of a novel bacteria-selective antimicrobial peptide from the cell-penetrating peptide Pep-1. Biochem. Biophys. Res. Commun. 2006; 349: 769-774.
    • (2006) Biochem. Biophys. Res. Commun , vol.349 , pp. 769-774
    • Zhu, W.L.1    Lan, H.2    Park, I.S.3    Kim, J.I.4    Jin, H.Z.5    Hahm, K.S.6    Shin, S.Y.7
  • 8
    • 33751094325 scopus 로고    scopus 로고
    • Effects of Pro→peptoid residue substitution on cell selectivity and mechanism of antibacterial action of tritrpticin-amide antimicrobial peptide
    • Zhu WL, Lan H, Park Y, Yang ST, Kim JI, Park IS, You HJ, Lee JS, Park YS, Kim Y, Hahm KS, Shin SY. Effects of Pro→peptoid residue substitution on cell selectivity and mechanism of antibacterial action of tritrpticin-amide antimicrobial peptide. Biochemistry 2006; 45: 13007-13017.
    • (2006) Biochemistry , vol.45 , pp. 13007-13017
    • Zhu, W.L.1    Lan, H.2    Park, Y.3    Yang, S.T.4    Kim, J.I.5    Park, I.S.6    You, H.J.7    Lee, J.S.8    Park, Y.S.9    Kim, Y.10    Hahm, K.S.11    Shin, S.Y.12
  • 10
    • 0021755639 scopus 로고
    • Differential light scattering and absorption flattening optical effects are minimal in the circular-dichroism spectra of small unilamellar vesicles
    • Mao D, Wallace BA. Differential light scattering and absorption flattening optical effects are minimal in the circular-dichroism spectra of small unilamellar vesicles. Biochemistry 1984; 23: 2667-2673.
    • (1984) Biochemistry , vol.23 , pp. 2667-2673
    • Mao, D.1    Wallace, B.A.2
  • 11
    • 0025245504 scopus 로고
    • Channel formation properties of synthetic pardaxin and analogues
    • Shai Y, Bach D, Yanovsky A. Channel formation properties of synthetic pardaxin and analogues. J. Biol. Chem. 1990; 265: 20202-20209.
    • (1990) J. Biol. Chem , vol.265 , pp. 20202-20209
    • Shai, Y.1    Bach, D.2    Yanovsky, A.3
  • 12
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • De Kroon AI, Soekarjo MW, De Gier J, De Kruijff B. The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers. Biochemistry 1990; 29: 8229-8240.
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • De Kroon, A.I.1    Soekarjo, M.W.2    De Gier, J.3    De Kruijff, B.4
  • 13
    • 0037067706 scopus 로고    scopus 로고
    • Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence
    • Zhao H, Kinnunen PK. Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J. Biol. Chem. 2002; 277: 25170-25177.
    • (2002) J. Biol. Chem , vol.277 , pp. 25170-25177
    • Zhao, H.1    Kinnunen, P.K.2
  • 14
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink MR, Ghiron CA. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry 1976; 15: 672-680.
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 15
    • 33847798446 scopus 로고
    • Fluorescence quenching of indole and model micelle systems
    • Eftink MR, Ghiron CA. Fluorescence quenching of indole and model micelle systems. J. Phys. Chem. 1976; 80: 486-493.
    • (1976) J. Phys. Chem , vol.80 , pp. 486-493
    • Eftink, M.R.1    Ghiron, C.A.2
  • 16
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Barlett CR. Phosphorus assay in column chromatography. J. Biol. Chem. 1959; 234: 466-468.
    • (1959) J. Biol. Chem , vol.234 , pp. 466-468
    • Barlett, C.R.1
  • 17
    • 0033915369 scopus 로고    scopus 로고
    • Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria
    • Friedrich CL, Moyles D, Beveridge TJ, Hancock RE. Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria. Antimicrob. Agents Chemother. 2000; 44: 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
  • 18
    • 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: 24015-24022.
    • (2001) J. Biol. Chem , vol.276 , pp. 24015-24022
    • Friedrich, C.L.1    Rozek, A.2    Patrzykat, A.3    Hancock, R.E.4
  • 19
    • 34548236882 scopus 로고    scopus 로고
    • Cathelicidin-derived Trp/Pro-rich antimicrobial peptides with lysine peptoid residue (Nlys): Therapeutic index and plausible mode of action
    • Zhu WL, Hahm KS, Shin SY. Cathelicidin-derived Trp/Pro-rich antimicrobial peptides with lysine peptoid residue (Nlys): therapeutic index and plausible mode of action. J. Pept. Sci. 2007; 13: 529-535.
    • (2007) J. Pept. Sci , vol.13 , pp. 529-535
    • Zhu, W.L.1    Hahm, K.S.2    Shin, S.Y.3
  • 21
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of a-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of a-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
  • 22
    • 34248377855 scopus 로고    scopus 로고
    • Biological and structural characterization of new linear gomesin analogues with improved therapeutic indices
    • Fazio MA, Jouvensal L, Vovelle F, Bulet P, Miranda MT, Daffre S, Miranda A. Biological and structural characterization of new linear gomesin analogues with improved therapeutic indices. Biopolymers 2007; 88: 386-400.
    • (2007) Biopolymers , vol.88 , pp. 386-400
    • Fazio, M.A.1    Jouvensal, L.2    Vovelle, F.3    Bulet, P.4    Miranda, M.T.5    Daffre, S.6    Miranda, A.7
  • 23
    • 34249070808 scopus 로고    scopus 로고
    • Substitution of the leucine zipper sequence inmelittin with peptoid residues affects self-association, cell selectivity, and mode of action
    • Zhu WL, Song YM, Park Y, Park KH, Yang ST, Kim JI, Park IS, Hahm KS, Shin SY. Substitution of the leucine zipper sequence inmelittin with peptoid residues affects self-association, cell selectivity, and mode of action. Biochim. Biophys. Acta 2007; 1768: 1506-1517.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1506-1517
    • Zhu, W.L.1    Song, Y.M.2    Park, Y.3    Park, K.H.4    Yang, S.T.5    Kim, J.I.6    Park, I.S.7    Hahm, K.S.8    Shin, S.Y.9
  • 24
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park CB, Kim HS, Kim SC. Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 1998; 244: 253-257.
    • (1998) Biochem. Biophys. Res. Commun , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 25
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • Park CB, Yi KS, Matsuzaki K, Kim MS, Kim SC. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl. Acad. Sci. U S A. 2000; 97: 8245-8250.
    • (2000) Proc. Natl. Acad. Sci. U S A , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 27
    • 0031022395 scopus 로고    scopus 로고
    • Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids
    • Ladokhin AS, Selsted ME, White SH. Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids. Biophys. J. 1997; 72: 794-805.
    • (1997) Biophys. J , vol.72 , pp. 794-805
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 28
    • 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
  • 29
    • 0030586288 scopus 로고    scopus 로고
    • Antimicrobial activity of a 13 amino acid tryptophanrich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides
    • Lawyer C, Pai S, Watabe M, Borgia P, Mashimo T, Eagleton L, Watabe K. Antimicrobial activity of a 13 amino acid tryptophanrich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides. FEBS Lett. 1996; 390: 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
  • 30
    • 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
  • 31
    • 0346034649 scopus 로고    scopus 로고
    • Tryptophan-rich antimicrobial peptides: Comparative properties and membrane interactions
    • Schibli DJ, Epand RF, Vogel HJ, Epand RM. Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions. Biochem. Cell Biol. 2002; 80: 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
  • 33
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • Matsuzaki K. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta 1998; 1376: 391-400.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 35
    • 0032763732 scopus 로고    scopus 로고
    • Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy
    • Marassi FM, Opella SJ, Juvvadi P, Merrifield RB. Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy. Biophys. J. 1999; 77: 3152-3155.
    • (1999) Biophys. J , vol.77 , pp. 3152-3155
    • Marassi, F.M.1    Opella, S.J.2    Juvvadi, P.3    Merrifield, R.B.4
  • 36
    • 0036252094 scopus 로고    scopus 로고
    • Pro-rich antimicrobial peptides from animals: Structure, biological functions and mechanism of action
    • Gennaro R, Zanetti M, Benincasa M, Podda E, Miani M. Pro-rich antimicrobial peptides from animals: structure, biological functions and mechanism of action. Curr. Pharm. Des. 2002; 8: 763-778.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 763-778
    • Gennaro, R.1    Zanetti, M.2    Benincasa, M.3    Podda, E.4    Miani, M.5
  • 37
    • 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


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