Co-assembly of human islet amyloid polypeptide (hIAPP)/insulin

Chem Commun (Camb). 2012 Jan 7;48(2):191-3. doi: 10.1039/c1cc14285b. Epub 2011 Oct 14.

Abstract

The pathogenesis of type II diabetes can be linked to cosecreted hIAPP/insulin interacting with cell membranes. Here we investigate the nanostructures by co-assembling hIAPP and insulin on surfaces. By tuning the hIAPP/insulin ratio, atomic force microscopy reveals the resulting nanostructure morphology changes from fibrils to oligomers, to annular. Implications for in vivo studies are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / metabolism
  • Amyloid / ultrastructure*
  • Diabetes Mellitus, Type 2 / metabolism*
  • Diabetes Mellitus, Type 2 / pathology
  • Humans
  • Insulin / metabolism*
  • Islet Amyloid Polypeptide / metabolism*
  • Microscopy, Atomic Force

Substances

  • Amyloid
  • Insulin
  • Islet Amyloid Polypeptide