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  • Title: Control of leakage activities of alamethicin analogs by metals: side chain-dependent adverse gating response to Zn(2+).
    Author: Noshiro D, Asami K, Futaki S.
    Journal: Bioorg Med Chem; 2012 Dec 01; 20(23):6870-6. PubMed ID: 23088911.
    Abstract:
    Alamethicin (Alm), an antimicrobial peptide rich in α-aminoisobutyric acid (Aib), is known to self-assemble to form channels in the membranes. Previously, we reported that HG-Alm, an Alm analog with a single His residue at the N-terminus, forms channel assemblies with extremely long lifetimes in the presence of Zn(2+). In this study, HG-Alm analogs, in the sequences of which all Aib residues were substituted by Leu, norvaline (Nva), or norleucine (Nle), were synthesized and their leakage activities were measured using fluorescent dye-loaded liposomes. We found that these peptides could be categorized into two classes with different gating responses to Zn(2+).
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