메뉴 건너뛰기




Volumn 1768, Issue 6, 2007, Pages 1506-1517

Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action

Author keywords

Antimicrobial peptide; Cell selectivity; Leucine zipper; Melittin; Peptoid residue; Self association

Indexed keywords

ALANINE; AMPHOLYTE; DODECYL SULFATE SODIUM; LEUCINE; LYSINE; MELITTIN; PEPTOID; PHENYLALANINE; POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 34249070808     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.03.010     Document Type: Article
Times cited : (76)

References (53)
  • 1
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13 (1995) 61-92
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 2
    • 0027474382 scopus 로고
    • Defensins: antimicrobial and cytotoxic peptides of mammalian cells
    • Lehrer R.I., Lichtenstein A.K., and Ganz T. Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11 (1993) 105-128
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 4
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature (London) 415 (2002) 389-395
    • (2002) Nature (London) , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 5
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock E.W., and Scott M.G. The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 8856-8861
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8856-8861
    • Hancock, E.W.1    Scott, M.G.2
  • 6
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: an overview
    • Andreu D., and Rivas L. Animal antimicrobial peptides: an overview. Biopolymers 47 (1998) 415-433
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 7
    • 0035958848 scopus 로고    scopus 로고
    • A novel linear amphipathic β-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids
    • Blazyk J., Wiegand R., Klein J., Hammer J., Epand R.M., Epand R.F., Maloy W.L., and Kari U.P. A novel linear amphipathic β-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids. J. Biol. Chem. 276 (2001) 27899-27906
    • (2001) J. Biol. Chem. , vol.276 , pp. 27899-27906
    • Blazyk, J.1    Wiegand, R.2    Klein, J.3    Hammer, J.4    Epand, R.M.5    Epand, R.F.6    Maloy, W.L.7    Kari, U.P.8
  • 8
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., and Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462 (1999) 71-87
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 9
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic α-helical antimicrobial peptides
    • Giangaspero A., Sandri L., and Tossi A. Amphipathic α-helical antimicrobial peptides. Eur. J. Biochem. 268 (2001) 5589-5600
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 10
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen Y., Mant C.T., Farmer S.W., Hancock R.E., Vasil M.L., and Hodges R.S. Rational design of α-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
  • 11
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, α-helical antimicrobial peptides
    • Tossi A., Sandri L., and Giangaspero A. Amphipathic, α-helical antimicrobial peptides. Biopolymers 55 (2000) 4-30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 12
    • 0037072808 scopus 로고    scopus 로고
    • The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers
    • Papo N., Oren Z., Pag U., Sahl H.G., and Shai Y. The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers. J. Biol. Chem. 277 (2002) 33913-33921
    • (2002) J. Biol. Chem. , vol.277 , pp. 33913-33921
    • Papo, N.1    Oren, Z.2    Pag, U.3    Sahl, H.G.4    Shai, Y.5
  • 13
    • 25844462488 scopus 로고    scopus 로고
    • Conjugation of fatty acids with different lengths modulates the antibacterial and antifungal activity of a cationic biologically inactive peptide
    • Malina A., and Shai Y. Conjugation of fatty acids with different lengths modulates the antibacterial and antifungal activity of a cationic biologically inactive peptide. Biochem. J. 390 (2005) 695-702
    • (2005) Biochem. J. , vol.390 , pp. 695-702
    • Malina, A.1    Shai, Y.2
  • 14
    • 0037053317 scopus 로고    scopus 로고
    • Structural requirements for potent versus selective cytotoxicity for antimicrobial dermaseptin S4 derivatives
    • Kustanovich I., Shalev D.E., Mikhlin M., Gaidukov L., and Mor A. Structural requirements for potent versus selective cytotoxicity for antimicrobial dermaseptin S4 derivatives. J. Biol. Chem. 277 (2002) 16941-16951
    • (2002) J. Biol. Chem. , vol.277 , pp. 16941-16951
    • Kustanovich, I.1    Shalev, D.E.2    Mikhlin, M.3    Gaidukov, L.4    Mor, A.5
  • 15
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell selective activity
    • Oren Z., Lerman J.C., Gudmundsson G.H., Agerberth B., and Shai Y. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell selective activity. Biochem. J. 341 (1999) 501-513
    • (1999) Biochem. J. , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 16
    • 0035940519 scopus 로고    scopus 로고
    • Effect of multiple aliphatic amino acids substitutions on the structure, function, and mode of action of diastereomeric membrane active peptides
    • Avrahami D., Oren Z., and Shai Y. Effect of multiple aliphatic amino acids substitutions on the structure, function, and mode of action of diastereomeric membrane active peptides. Biochemistry 40 (2001) 12591-12603
    • (2001) Biochemistry , vol.40 , pp. 12591-12603
    • Avrahami, D.1    Oren, Z.2    Shai, Y.3
  • 17
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of antibacterial and toxic activity of melittin: a leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity
    • Asthana N., Yadav S.P., and Ghosh J.K. Dissection of antibacterial and toxic activity of melittin: a leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity. J. Biol. Chem. 279 (2004) 55042-55050
    • (2004) J. Biol. Chem. , vol.279 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 18
    • 0033594986 scopus 로고    scopus 로고
    • Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides
    • Zhang L., Benz R., and Hancock R.E. Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides. Biochemistry 38 (1999) 8102-8111
    • (1999) Biochemistry , vol.38 , pp. 8102-8111
    • Zhang, L.1    Benz, R.2    Hancock, R.E.3
  • 19
    • 0347635410 scopus 로고    scopus 로고
    • Effects of L- or D-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic α-helical model peptide on structure and cell selectivity
    • Song Y.M., Yang S.-T., Lim S.S., Kim Y., Hahm K.-S., Kim J.I., and Shin S.Y. Effects of L- or D-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic α-helical model peptide on structure and cell selectivity. Biochem. Biophys. Res. Commun. 314 (2004) 615-621
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 615-621
    • Song, Y.M.1    Yang, S.-T.2    Lim, S.S.3    Kim, Y.4    Hahm, K.-S.5    Kim, J.I.6    Shin, S.Y.7
  • 20
    • 4544349379 scopus 로고    scopus 로고
    • Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs
    • Lee K., Shin S.Y., Kim K., Lim S.S., Hahm K.-S., and Kim Y. Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs. Biochem. Biophys. Res. Commun. 323 (2004) 712-719
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 712-719
    • Lee, K.1    Shin, S.Y.2    Kim, K.3    Lim, S.S.4    Hahm, K.-S.5    Kim, Y.6
  • 21
    • 33747432947 scopus 로고    scopus 로고
    • Contribution of a central proline in model amphipathic α-helical peptides to self-association, interaction with phospholipids, and antimicrobial mode of action
    • Yang S.-T., Lee J.Y., Kim H.J., Eu Y.J., Shin S.Y., Hahm K.-S., and Kim J.I. Contribution of a central proline in model amphipathic α-helical peptides to self-association, interaction with phospholipids, and antimicrobial mode of action. FEBS J. 273 (2006) 4040-4054
    • (2006) FEBS J. , vol.273 , pp. 4040-4054
    • Yang, S.-T.1    Lee, J.Y.2    Kim, H.J.3    Eu, Y.J.4    Shin, S.Y.5    Hahm, K.-S.6    Kim, J.I.7
  • 22
    • 0037111314 scopus 로고    scopus 로고
    • Hydrophobicity and helicity of membrane-interactive peptides containing peptoid residues
    • Tang Y.C., and Deber C.M. Hydrophobicity and helicity of membrane-interactive peptides containing peptoid residues. Biopolymers 65 (2002) 254-262
    • (2002) Biopolymers , vol.65 , pp. 254-262
    • Tang, Y.C.1    Deber, C.M.2
  • 23
    • 1942531294 scopus 로고    scopus 로고
    • Aqueous solubility and membrane interactions of hydrophobic peptides with peptoid tags
    • Tang Y.C., and Deber C.M. Aqueous solubility and membrane interactions of hydrophobic peptides with peptoid tags. Biopolymers 76 (2004) 110-118
    • (2004) Biopolymers , vol.76 , pp. 110-118
    • Tang, Y.C.1    Deber, C.M.2
  • 25
    • 0023792919 scopus 로고
    • Evaluation of a soluble tetrazolium/formazan assay for cell growth and drug sensitivity in culture using human and other tumor cell lines
    • Scudiero D.A., Shoemaker R.H., Paull K.D., Monks A., Tierney S., Nofziger T.H., Currens M.J., Seniff D., and Boyd M.R. Evaluation of a soluble tetrazolium/formazan assay for cell growth and drug sensitivity in culture using human and other tumor cell lines. Cancer Res. 48 (1988) 4827-4833
    • (1988) Cancer Res. , vol.48 , pp. 4827-4833
    • Scudiero, D.A.1    Shoemaker, R.H.2    Paull, K.D.3    Monks, A.4    Tierney, S.5    Nofziger, T.H.6    Currens, M.J.7    Seniff, D.8    Boyd, M.R.9
  • 26
    • 0021755639 scopus 로고
    • Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles
    • Mao D., and Wallace B.A. Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry 23 (1984) 2667-2673
    • (1984) Biochemistry , vol.23 , pp. 2667-2673
    • Mao, D.1    Wallace, B.A.2
  • 27
    • 0025245504 scopus 로고
    • Channel formation properties of synthetic pardaxin and analogues
    • Shai Y., Bach D., and Yanovsky A. Channel formation properties of synthetic pardaxin and analogues. J. Biol. Chem. 265 (1990) 20202-20209
    • (1990) J. Biol. Chem. , vol.265 , pp. 20202-20209
    • Shai, Y.1    Bach, D.2    Yanovsky, A.3
  • 28
    • 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 A.I., Soekarjo M.W., De Gier J., and 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 29 (1990) 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
  • 29
    • 0037067706 scopus 로고    scopus 로고
    • Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence
    • Zhao H., and Kinnunen P.K. Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J. Biol. Chem. 277 (2002) 25170-25177
    • (2002) J. Biol. Chem. , vol.277 , pp. 25170-25177
    • Zhao, H.1    Kinnunen, P.K.2
  • 30
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Barlett C.R. Phosphorus assay in column chromatography. J. Biol. Chem. 234 (1959) 466-468
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Barlett, C.R.1
  • 31
    • 0033915369 scopus 로고    scopus 로고
    • Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria
    • Friedrich C.L., Moyles D., Beveridge T.J., and Hancock R.E. 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
  • 32
    • 0035968224 scopus 로고    scopus 로고
    • Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria
    • Friedrich C.L., Rozek A., Patrzykat A., and Hancock R.E. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria. J. Biol. Chem. 276 (2001) 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
  • 33
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • Zhang L., Rozek A., and Hancock R.E. 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
  • 34
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki K., Murase O., Fujii N., and Miyajima K. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35 (1996) 11361-11368
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 35
    • 0034713613 scopus 로고    scopus 로고
    • Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: proline as a translocation promoting factor
    • Kobayashi S., Takeshima K., Park C.B., Kim S.C., and Matsuzaki K. Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: proline as a translocation promoting factor. Biochemistry 39 (2000) 8648-8654
    • (2000) Biochemistry , vol.39 , pp. 8648-8654
    • Kobayashi, S.1    Takeshima, K.2    Park, C.B.3    Kim, S.C.4    Matsuzaki, K.5
  • 36
    • 0029797094 scopus 로고    scopus 로고
    • Design and synthesis of amphiphilic α-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes
    • Kiyota T., Lee S., and Sugihara G. Design and synthesis of amphiphilic α-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes. Biochemistry 35 (1996) 13196-13204
    • (1996) Biochemistry , vol.35 , pp. 13196-13204
    • Kiyota, T.1    Lee, S.2    Sugihara, G.3
  • 37
    • 0028113997 scopus 로고
    • Reversed-phase chromatography of synthetic amphipathic α-helical peptides as a model for ligand/receptor interactions. Effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains
    • Sereda T.J., Mant C.T., Sonnichsen F.D., and Hodges S. Reversed-phase chromatography of synthetic amphipathic α-helical peptides as a model for ligand/receptor interactions. Effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains. J. Chromatogr., A 676 (1994) 139-153
    • (1994) J. Chromatogr., A , vol.676 , pp. 139-153
    • Sereda, T.J.1    Mant, C.T.2    Sonnichsen, F.D.3    Hodges, S.4
  • 38
    • 0019332396 scopus 로고
    • High-resolution 1H-NMR studies of self-aggregation of melittin in aqueous solution
    • Brown L.R., Lauterwein J., and Wuthrich K. High-resolution 1H-NMR studies of self-aggregation of melittin in aqueous solution. Biochim. Biophys. Acta 622 (1980) 231-244
    • (1980) Biochim. Biophys. Acta , vol.622 , pp. 231-244
    • Brown, L.R.1    Lauterwein, J.2    Wuthrich, K.3
  • 39
    • 0020712137 scopus 로고
    • Conformational studies of aqueous melittin: thermodynamic parameters of the monomer-tetramer self-association reaction
    • Quay S.C., and Condie C.C. Conformational studies of aqueous melittin: thermodynamic parameters of the monomer-tetramer self-association reaction. Biochemistry 22 (1983) 695-700
    • (1983) Biochemistry , vol.22 , pp. 695-700
    • Quay, S.C.1    Condie, C.C.2
  • 40
    • 0026684928 scopus 로고
    • Similarities in melittin functional group reactivities during self-association and association with lipid bilayers
    • Oomen R.P., and Kaplan H. Similarities in melittin functional group reactivities during self-association and association with lipid bilayers. Biochemistry 31 (1992) 5698-5704
    • (1992) Biochemistry , vol.31 , pp. 5698-5704
    • Oomen, R.P.1    Kaplan, H.2
  • 41
    • 33749008521 scopus 로고    scopus 로고
    • Effect of ionic strength on folding and aggregation of the hemolytic peptide melittin in solution
    • Raghuraman H., and Chattopadhyay A. Effect of ionic strength on folding and aggregation of the hemolytic peptide melittin in solution. Biopolymers 83 (2006) 111-121
    • (2006) Biopolymers , vol.83 , pp. 111-121
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 42
    • 33745908271 scopus 로고    scopus 로고
    • Improvement of bacterial cell selectivity of melittin by a single Trp mutation with a peptoid residue
    • Zhu W.L., Park Y., Park I.-S., Park Y.S., Kim Y., Hahm K.-S., and Shin S.Y. Improvement of bacterial cell selectivity of melittin by a single Trp mutation with a peptoid residue. Protein Pept. Lett. 13 (2006) 719-725
    • (2006) Protein Pept. Lett. , vol.13 , pp. 719-725
    • Zhu, W.L.1    Park, Y.2    Park, I.-S.3    Park, Y.S.4    Kim, Y.5    Hahm, K.-S.6    Shin, S.Y.7
  • 43
    • 0035479424 scopus 로고    scopus 로고
    • 'Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • Ladokhin A.S., and White S.H. 'Detergent-like' permeabilization of anionic lipid vesicles by melittin. Biochim. Biophys. Acta 1514 (2001) 253-260
    • (2001) Biochim. Biophys. Acta , vol.1514 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 44
    • 0030971376 scopus 로고    scopus 로고
    • Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin
    • Ladokhin A.S., Selsted M.E., and White S.H. Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin. Biophys. J. 72 (1997) 1762-1766
    • (1997) Biophys. J. , vol.72 , pp. 1762-1766
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 45
    • 0037457824 scopus 로고    scopus 로고
    • Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides
    • Papo N., and Shai Y. Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides. Biochemistry 42 (2003) 458-466
    • (2003) Biochemistry , vol.42 , pp. 458-466
    • Papo, N.1    Shai, Y.2
  • 46
    • 1042267410 scopus 로고    scopus 로고
    • Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes?
    • Papo N., and Shai Y. Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes?. Peptides 24 (2003) 1693-1703
    • (2003) Peptides , vol.24 , pp. 1693-1703
    • Papo, N.1    Shai, Y.2
  • 47
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • Shai Y., and Oren Z. From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides. Peptides 22 (2001) 1629-1641
    • (2001) Peptides , vol.22 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 48
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., and Vogel H.J. 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
  • 49
    • 33644856596 scopus 로고    scopus 로고
    • Mechanistic and functional studies of the interaction of a proline-rich antimicrobial peptide with mammalian cells
    • Tomasinsig L., Skerlavaj B., Papo N., Giabbai B., Shai Y., and Zanetti M. Mechanistic and functional studies of the interaction of a proline-rich antimicrobial peptide with mammalian cells. J. Biol. Chem. 281 (2006) 383-391
    • (2006) J. Biol. Chem. , vol.281 , pp. 383-391
    • Tomasinsig, L.1    Skerlavaj, B.2    Papo, N.3    Giabbai, B.4    Shai, Y.5    Zanetti, M.6
  • 50
    • 0036214967 scopus 로고    scopus 로고
    • Intracellular targets of antibacterial peptides
    • Cudic M., and Otvos Jr. L. Intracellular targets of antibacterial peptides. Curr. Drug Targets 3 (2002) 101-106
    • (2002) Curr. Drug Targets , vol.3 , pp. 101-106
    • Cudic, M.1    Otvos Jr., L.2
  • 51
    • 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 C.B., Yi K.S., Matsuzaki K., Kim M.S., and Kim S.C. 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. 97 (2000) 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
  • 52
    • 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 C.B., Kim H.S., and Kim S.C. 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. 244 (1998) 253-257
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 53
    • 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 W.L., Lan H., Park I.-S., Kim J.I., Jin H.Z., Hahm K.-S., and Shin S.Y. Design and mechanism of action of a novel bacteria-selective antimicrobial peptide from the cell-penetrating peptide Pep-1. Biochem. Biophys. Res. Commun. 349 (2006) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.