title: Effect of Zn(2+) ions on the assembly of amylin oligomers: insight into the molecular mechanisms.
abstract: Amylin is an endocrine hormone and is a member of the family of amyloid peptides and proteins that emerge as potential scaffolds by self-assembly processes. Zn(2+) ions can bind to amylin peptides to form self-assembled Zn(2+)-amylin oligomers. In the current work the binding sites of Zn(2+) ions in the self-assembled amylin oligomers at various concentrations of zinc have been investigated. Our results yield two conclusions. First, in the absence of Zn(2+) ions polymorphic states (i.e. various classes of amylin oligomers) are obtained, but when Zn(2+) ions bind to amylin peptides to form Zn(2+)-amylin oligomers, the polymorphism is decreased, i.e. Zn(2+) ions bind only to specific classes of amylin. At low concentrations of Zn(2+) ions the polymorphism is smaller than at high concentrations. Second, the structural features of the self-assembled amylin oligomers are not affected by the presence of Zn(2+) ions. This study proposes new molecular mechanisms of the self-assembly of Zn(2+)-amylin oligomers.
authors.affiliation: Department of Chemistry, Ben-Gurion University of the Negev, P.O. Box 653, Be'er Sheva 84105, Israel. ymiller@bgu.ac.il and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, Beér-Sheva 84105, Israel.
authors.forename: Vered
authors.initials: V
authors.lastname: Wineman-Fisher
authors.affiliation: Department of Chemistry, Ben-Gurion University of the Negev, P.O. Box 653, Be'er Sheva 84105, Israel. ymiller@bgu.ac.il and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, Beér-Sheva 84105, Israel.
authors.forename: Yifat
authors.initials: Y
authors.lastname: Miller
mesh_terms: D000818:Animals; D001665:Binding Sites; D006801:Humans; D058228:Islet Amyloid Polypeptide / Q000737:chemistry*; D015032:Zinc
chemical_list: D058228:Islet Amyloid Polypeptide; D015032:Zinc