Antimicrobial peptides are used as the first defensive barrier of the organism against microbial infection. They possess positive charge, a substantial portion of hydrophobic residues and adopt amphipathic conformations when interacting with bacterial membranes. Our approach is based on the design, synthesis and study of helical sequential polypeptides (Arg-X-Gly)_n, where X = Ala, Val, Leu and amphipathic Aib-containing peptide models of various chain-lengths, Ac-(Aib-Arg-Aib-Leu)_n-NH2 (n = 1 - 4). The presence of Aib, which induces and stabilizes helical structures, in combination with the hydrophobic amino-acids and the positive charge of Arg side-chain, for the interaction with the negatively charged phospholipid membranes, target to the development of new antimicrobial peptides.
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