期刊
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
卷 45, 期 3, 页码 195-207出版社
SPRINGER
DOI: 10.1007/s00249-015-1094-x
关键词
Antimicrobial peptides; Membrane; Molecular dynamics; Secondary structure; Cooperative effect; Amino acid; Anticancer
类别
资金
- Volkswagen Foundation (Germany) [83932]
Aurein 2.6-COOH and aurein 3.1-COOH were studied along with their naturally occurring C-terminally amidated analogues. Circular dichroism (CD) and molecular dynamic (MD) simulations were used to study the effects of amidation on the interaction of antimicrobial peptides (AMPs) with lipid bilayers. CD measurements and MD analysis suggested that both peptide analogues were predominantly random coil and adopted low levels of -helical structure in solution (< 30 %) and in the presence of a lipid bilayer the peptides formed a stable -helical structure. In general, amidated analogues have a greater propensity than the non-amidated peptides to form a -helical structure. MD simulations predicted that aurein 2.6-COOH and aurein 3.1-CHOOH destabilised lipid bilayers from 1,2-dimyristoyl-sn-glycero-3-phosphocholine and 1,2-dimyristoyl-sn-glycero-3-phosphoserine via angled bilayer penetration. They also showed that aurein 2.6-CONH and aurein 3.1-CONH formed a helix horizontal to the plane of an asymmetric interface.
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