Effect of Zn2+ ions on the assembly of amylin oligomers: insight into the molecular mechanisms. Issue 31 (18th July 2016)

• Record Type: Journal Article
• Authors: Wineman-Fisher, Vered; Miller, Yifat
• Is Part Of: Physical chemistry chemical physics. Volume 18:Issue 31(2016)
• Page Start: 21590
• Page End: 21599
• Publication Date: 2016-07-18
• Subjects: Chemistry, Physical and theoretical -- Periodicals; 541.3
• DOI: 10.1039/c6cp04105a
• Languages: English
• ISSNs: 1463-9076

Abstract

Abstract : High and low concentrations of Zn 2+ ions decrease the polymorphism of amylin oligomers and do not affect their cross β-beta structures. 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.