Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

Chem Commun (Camb). 2013 Apr 25;49(32):3339-41. doi: 10.1039/c3cc40383a.

Abstract

The aggregation of human islet amyloid polypeptide (hIAPP) has been linked to beta-cell death in type II diabetes. Zinc present in secretory granules has been shown to affect this aggregation. A combination of EXAFS, NMR, and AFM experiments shows that the influence of zinc is most likely due to the stabilization of prefibrillar aggregates of hIAPP.

MeSH terms

  • Humans
  • Islet Amyloid Polypeptide / chemistry*
  • Microscopy, Atomic Force
  • X-Ray Absorption Spectroscopy
  • Zinc / chemistry*

Substances

  • Islet Amyloid Polypeptide
  • Zinc