Effect of Zn2+ ions on the assembly of amylin oligomers: Insight into the molecular mechanisms

Vered Wineman-Fisher, Yifat Miller

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

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. Zn2+ ions can bind to amylin peptides to form self-assembled Zn2+-amylin oligomers. In the current work the binding sites of Zn2+ 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 Zn2+ ions polymorphic states (i.e. various classes of amylin oligomers) are obtained, but when Zn2+ ions bind to amylin peptides to form Zn2+-amylin oligomers, the polymorphism is decreased, i.e. Zn2+ ions bind only to specific classes of amylin. At low concentrations of Zn2+ 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 Zn2+ ions. This study proposes new molecular mechanisms of the self-assembly of Zn2+-amylin oligomers.

Original languageEnglish
Pages (from-to)21590-21599
Number of pages10
JournalPhysical Chemistry Chemical Physics
Volume18
Issue number31
DOIs
StatePublished - 1 Jan 2016

ASJC Scopus subject areas

  • Physics and Astronomy (all)
  • Physical and Theoretical Chemistry

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