TY - JOUR
T1 - Not only the nature of peptide but also the characteristics of cell membrane determine the antimicrobial mechanism of a peptide
AU - Liang, Jun F.
AU - Kim, S. C.
PY - 1999
Y1 - 1999
N2 - 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 AD 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.
AB - 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 AD 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.
KW - Antimicrobial
KW - Electroporation
KW - Escherichia coli
KW - Mechanism
KW - Peptide
UR - http://www.scopus.com/inward/record.url?scp=0033037847&partnerID=8YFLogxK
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U2 - 10.1034/j.1399-3011.1999.00051.x
DO - 10.1034/j.1399-3011.1999.00051.x
M3 - Article
C2 - 10424346
AN - SCOPUS:0033037847
SN - 1397-002X
VL - 53
SP - 518
EP - 522
JO - Journal of Peptide Research
JF - Journal of Peptide Research
IS - 5
ER -