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KMID : 0624620090420090586
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BMB Reports
2009 Volume.42 No. 9 p.586 ~ p.592
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Different modes of antibiotic action of homodimeric and monomeric bactenecin, a cathelicidin-derived antibacterial peptide
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Lee Ju-Yeon
Yang Sung-Tae
Kim Hyo-Jeong
Lee Seung-Kyu
Jung Hyun-Ho
Shin Song-Yub
Kim Jae-Il
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Abstract
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The bactenecin is an antibacterial peptide with an intramolecular disulfide bond. We recently found that homodimeric bactenecin exhibits more potent antibacterial activity than the monomeric form and retains its activity at physiological conditions. Here we assess the difference in the modes of antibiotic action of homodimeric and monomeric bactenecins. Both monomeric and dimeric bactenecins almost completely killed both Staphylococcus aureus and E. coli within 10-30 min at concentrations of 8-16 μM. However, exposure to liposomes elicited an increase in the fluorescence quantum yield from a tryptophan-containing monomeric analog, while the homodimeric analog showed a significant reduction in fluorescence intensity. Moreover, unlike the monomer, the homodimer displayed apparent membrane-lytic activity enabling release of various sized dyes from liposomes, and rapidly and fully depolarized the S. aureus membrane. Together, our results suggest that homodimeric bactenecin forms pores in the bacterial membrane, while monomeric one penetrates through the membrane to target intracellular molecules/organelles.
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KEYWORD
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Antibacterial activity, Homodimeric bactenecin, Model membrane, Monomeric bactenecin, Oligomerization
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