Not only the nature of peptide but also the characteristics of cell membrane determine the antimicrobial mechanism of a peptide

Journal of Peptide Research

Volumn 53, Issue 5, 1999, Pages 518-522

  Liang, Jun F ^a,c   Kim, S C ^b  

^a TSINGHUA UNIVERSITY   (China)

^b Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

^c UNIVERSITY OF MICHIGAN   (United States)

Author keywords

Antimicrobial; Electroporation; Escherichia coli; Mechanism; Peptide

Indexed keywords

ANTIBIOTIC AGENT; BUFORIN II; MAGAININ 2; POLYLYSINE; UNCLASSIFIED DRUG;

ANTIBACTERIAL ACTIVITY; ARTICLE; BACTERIAL GROWTH; DRUG DETERMINATION; DRUG POTENCY; ELECTROPORATION; ESCHERICHIA COLI; GROWTH INHIBITION; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; BACILLUS SUBTILIS; CELL MEMBRANE; DRUG RESISTANCE, MICROBIAL; ELECTROPORATION; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; PEPTIDES; POLYLYSINE; PROTEINS; PSEUDOMONAS PUTIDA; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS PROTEINS;

EID: 0033037847     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00051.x     Document Type: Article

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