Journal
EUROPEAN JOURNAL OF BIOCHEMISTRY
Volume 270, Issue 6, Pages 1240-1248Publisher
WILEY
DOI: 10.1046/j.1432-1033.2003.03484.x
Keywords
beta-peptide; antimicrobial; peptide-lipid interactions; membrane leakage; membrane intrinsic curvature
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Funding
- NIGMS NIH HHS [GM56414] Funding Source: Medline
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We have studied the interaction of beta-17, a potent synthetic antimicrobial beta-peptide, with phospholipids. We find that unlike other antimicrobial peptides such as magainin II, beta-17 facilitates the formation of nonbilayer phases, indicating that the peptide promotes negative curvature. Studies of liposomal leakage also indicate a different mode of membrane interaction relative to magainin II, but both leakage and membrane binding show that beta-17, like magainin II, has strong affinity for membranes containing anionic lipids. This is likely to be an important factor contributing to the antimicrobial specificity of the beta-peptide.
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