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

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The mechanisms of antimicrobial actions of magainin 2, buforin II and poly L-lysine against various Escherichia coli strains were studied. Poly L-lysine inhibited BL21, AD 434 and GroE(+)/DnaK(+) growth without lysing the cell. Magainin 2 had a pore-forming activity on BL 21 and ao 434 membrane but could not inhibit the GroE(+)/DnaK(+) growth in a nutrient-rich medium. Buforin II, which killed BL21 and AD 434 without cell membrane damage, lysed GroE+/DnaK+ to death. Once they were introduced into the cell by electroporation, all three peptides were able to inhibit cell growth at concentrations of 10 times lower than their MICs. These results indicate that the nature of the peptide and also the characteristics of the cell membrane determine the antimicrobial actions of a peptide.
Publisher
Springer
Issue Date
1999-05
Language
ENG
Article Type
Article
Keywords

ANTIBACTERIAL PEPTIDES; ESCHERICHIA-COLI; PORE; MAGAININ-2; SKIN

Citation

INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS, v.53, no.5, pp.518 - 522

ISSN
1573-3149
URI
http://hdl.handle.net/10203/74803
Appears in Collection
BS-Journal Papers(저널논문)
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