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Volumn 398, Issue 3, 2010, Pages 594-600

Novel short antibacterial and antifungal peptides with low cytotoxicity: Efficacy and action mechanisms

Author keywords

Helix; Antimicrobial peptides; Hydrophobicity; Pathogens

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; ANTIFUNGAL AGENT; ANTIINFECTIVE AGENT; ARGININE; DYE; GLYCINE; ISOLEUCINE; LEUCINE; LYSINE; MEMBRANE LIPID; PEPTIDE DERIVATIVE; PHENYLALANINE;

EID: 77955279662     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.06.131     Document Type: Article
Times cited : (62)

References (29)
  • 1
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: effectors in innate immunity and novel antimicrobials
    • Hancock R.E. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 2001, 1:156-164.
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 2
    • 0036834373 scopus 로고    scopus 로고
    • The future challenges facing the development of new antimicrobial drugs
    • Coates A., Hu Y., Bax R., Page C. The future challenges facing the development of new antimicrobial drugs. Nat. Rev. Drug Discov. 2002, 1:895-910.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 895-910
    • Coates, A.1    Hu, Y.2    Bax, R.3    Page, C.4
  • 3
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock R.E.W., Sahl H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 2006, 24:1551-1557.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.G.2
  • 4
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock R.E., Scott M.G. The role of antimicrobial peptides in animal defenses. Proc. Natl Acad. Sci. USA 2000, 97:8856-8861.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 5
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • Hilpert K., Volkmer-Engert R., Walter T., Hancock R.E. High-throughput generation of small antibacterial peptides with improved activity. Nat. Biotechnol. 2005, 23:1008-1012.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.4
  • 6
    • 33750446295 scopus 로고    scopus 로고
    • Ultrashort antibacterial and antifungal lipopeptides
    • Makovitzki A., Avrahami D., Shai Y. Ultrashort antibacterial and antifungal lipopeptides. Proc. Natl Acad. Sci. USA 2006, 103:15997-16002.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 15997-16002
    • Makovitzki, A.1    Avrahami, D.2    Shai, Y.3
  • 8
    • 33644926727 scopus 로고    scopus 로고
    • Solution structure of a novel tryptophan-rich peptide with bidirectional antimicrobial activity
    • Wei S.Y., Wu J.M., Kuo Y.Y., Chen H.L., Yip B.S., Tzeng S.R., Cheng J.W. Solution structure of a novel tryptophan-rich peptide with bidirectional antimicrobial activity. J. Bacteriol. 2006, 188:328-334.
    • (2006) J. Bacteriol. , vol.188 , pp. 328-334
    • Wei, S.Y.1    Wu, J.M.2    Kuo, Y.Y.3    Chen, H.L.4    Yip, B.S.5    Tzeng, S.R.6    Cheng, J.W.7
  • 9
    • 33646576163 scopus 로고    scopus 로고
    • Inhibition of plant-pathogenic bacteria by short synthetic cecropin A-melittin hybrid peptides
    • Ferre R., Badosa E., Feliu L., Planas M., Montesinos E., Bardaji E. Inhibition of plant-pathogenic bacteria by short synthetic cecropin A-melittin hybrid peptides. Appl. Environ. Microbiol. 2006, 72:3302-3308.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3302-3308
    • Ferre, R.1    Badosa, E.2    Feliu, L.3    Planas, M.4    Montesinos, E.5    Bardaji, E.6
  • 10
    • 77955280834 scopus 로고    scopus 로고
    • Clinical and Laboratory Standards Institute, I. Clinical and Laboratory Standards, Performance standards for antimicrobial susceptibility testing, CLSI document M100-S16, Clinical and Laboratory Standards Institute, Wayne, PA
    • Clinical and Laboratory Standards Institute, I. Clinical and Laboratory Standards, Performance standards for antimicrobial susceptibility testing, CLSI document M100-S16, vol. 188, Clinical and Laboratory Standards Institute, Wayne, PA, 2005, pp. 328-334.
    • (2005) , vol.188 , pp. 328-334
  • 11
    • 48249123462 scopus 로고    scopus 로고
    • Bacterial selectivity and plausible mode of antibacterial action of designed Pro-rich short model antimicrobial peptides
    • Park K.H., Park Y., Park I.S., Hahm K.S., Shin S.Y. 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
  • 12
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 1983, 65:55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 13
    • 67749088347 scopus 로고    scopus 로고
    • Imcroporin, a new cationic antimicrobial peptide from the venom of the scorpion Isometrus maculates
    • Zhao Z., Ma Y., Dai C., Zhao R., Li S., Wu Y., Cao Z., Li W. Imcroporin, a new cationic antimicrobial peptide from the venom of the scorpion Isometrus maculates. Antimicrob. Agents Chemother. 2009, 53:3472-3477.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 3472-3477
    • Zhao, Z.1    Ma, Y.2    Dai, C.3    Zhao, R.4    Li, S.5    Wu, Y.6    Cao, Z.7    Li, W.8
  • 14
    • 33748933561 scopus 로고    scopus 로고
    • Alpha-helical antimicrobial peptides - using a sequence template to guide structure-activity relationship studies
    • Zelezetsky I., Tossi A. Alpha-helical antimicrobial peptides - using a sequence template to guide structure-activity relationship studies. Biochim. Biophys. Acta - Biomembr. 2006, 1758:1436-1449.
    • (2006) Biochim. Biophys. Acta - Biomembr. , vol.1758 , pp. 1436-1449
    • Zelezetsky, I.1    Tossi, A.2
  • 15
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations
    • Melo M.N., Ferre R., Castanho M.A. Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol. 2009, 7:245-250.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.3
  • 16
    • 48249157851 scopus 로고    scopus 로고
    • Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes
    • Rathinakumar R., Wimley W.C. Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes. J. Am. Chem. Soc. 2008, 130:9849-9858.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9849-9858
    • Rathinakumar, R.1    Wimley, W.C.2
  • 17
    • 14744270888 scopus 로고    scopus 로고
    • Structural biology. Membrane protein insertion and stability
    • Mackinnon R. Structural biology. Membrane protein insertion and stability. Science 2005, 307:1425-1426.
    • (2005) Science , vol.307 , pp. 1425-1426
    • Mackinnon, R.1
  • 18
    • 0037202210 scopus 로고    scopus 로고
    • Structure-activity studies of 14-helical antimicrobial beta-peptides: probing the relationship between conformational stability and antimicrobial potency
    • Raguse T.L., Porter E.A., Weisblum B., Gellman S.H. Structure-activity studies of 14-helical antimicrobial beta-peptides: probing the relationship between conformational stability and antimicrobial potency. J. Am. Chem. Soc. 2002, 124:12774-12785.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12774-12785
    • Raguse, T.L.1    Porter, E.A.2    Weisblum, B.3    Gellman, S.H.4
  • 19
    • 27944443662 scopus 로고    scopus 로고
    • Tuning the biological properties of amphipathic alpha-helical antimicrobial peptides: rational use of minimal amino acid substitutions
    • Zelezetsky I., Pag U., Sahl H.G., Tossi A. Tuning the biological properties of amphipathic alpha-helical antimicrobial peptides: rational use of minimal amino acid substitutions. Peptides 2005, 26:2368-2376.
    • (2005) Peptides , vol.26 , pp. 2368-2376
    • Zelezetsky, I.1    Pag, U.2    Sahl, H.G.3    Tossi, A.4
  • 20
    • 0030949875 scopus 로고    scopus 로고
    • Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman M.J., Anderson G.M., Stolzenberg E.D., Kari U.P., Zasloff M., Wilson J.M. Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 1997, 88:553-560.
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 21
    • 1842639632 scopus 로고    scopus 로고
    • Helix stability confers salt resistance upon helical antimicrobial peptides
    • Park I.Y., Cho J.H., Kim K.S., Kim Y.B., Kim M.S., Kim S.C. Helix stability confers salt resistance upon helical antimicrobial peptides. J. Biol. Chem. 2004, 279:13896-13901.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13896-13901
    • Park, I.Y.1    Cho, J.H.2    Kim, K.S.3    Kim, Y.B.4    Kim, M.S.5    Kim, S.C.6
  • 23
    • 37849047198 scopus 로고    scopus 로고
    • Antimicrobial activity and protease stability of peptides containing fluorinated amino acids
    • Meng H., Kumar K. Antimicrobial activity and protease stability of peptides containing fluorinated amino acids. J. Am. Chem. Soc. 2007, 129:15615-15622.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15615-15622
    • Meng, H.1    Kumar, K.2
  • 24
    • 0020996054 scopus 로고
    • Electrogenic nature of lysosomal proton pump as revealed with a cyanine dye
    • Ohkuma S., Moriyama Y., Takano T. Electrogenic nature of lysosomal proton pump as revealed with a cyanine dye. J. Biochem. 1983, 94:1935-1943.
    • (1983) J. Biochem. , vol.94 , pp. 1935-1943
    • Ohkuma, S.1    Moriyama, Y.2    Takano, T.3
  • 27
    • 41549149586 scopus 로고    scopus 로고
    • Biomolecular simulations of membranes: physical properties from different force fields
    • Siu S.W.I., Vacha R., Jungwirth P., Bockmann R.A. Biomolecular simulations of membranes: physical properties from different force fields. J. Chem. Phys. 2008, 128:125103-125112.
    • (2008) J. Chem. Phys. , vol.128 , pp. 125103-125112
    • Siu, S.W.I.1    Vacha, R.2    Jungwirth, P.3    Bockmann, R.A.4
  • 28
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1999, 1462:71-87.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 29
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 2002, 66:236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1


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