title: Control of leakage activities of alamethicin analogs by metals: side chain-dependent adverse gating response to Zn(2+).
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+).
authors.affiliation: Institute for Chemical Research, Kyoto University, Uji, Kyoto, Japan.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Noshiro
authors.forename: Koji
authors.initials: K
authors.lastname: Asami
authors.forename: Shiroh
authors.initials: S
authors.lastname: Futaki
mesh_terms: D000408:Alamethicin / Q000031:analogs & derivatives* / Q000494:pharmacology*; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology*; D002942:Circular Dichroism; D007476:Ionophores / Q000737:chemistry* / Q000494:pharmacology*; D008081:Liposomes / Q000378:metabolism; D008969:Molecular Sequence Data; D015032:Zinc / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D007476:Ionophores; D008081:Liposomes; D000408:Alamethicin; D015032:Zinc