A membrane-bound antiparallel dimer of rat islet amyloid polypeptide

Angew Chem Int Ed Engl. 2011 Nov 11;50(46):10859-62. doi: 10.1002/anie.201102887. Epub 2011 Sep 22.

Abstract

A Membrane-bound Antiparallel Dimer of Rat Islet Amyloid Polypeptide IAPP, an amyloidogenic peptide linked to type 2 diabetes, forms a heterogeneous mixture of membrane-bound oligomers implicated in cytotoxicity and fibril formation. Structural characterization of these species has been a long-standing problem. Here, we examine the structure of a previously unrecognized antiparallel dimer of rat IAPP bound to anionic membrane Nanodiscs, using a novel combination of single-pair FRET and Rosetta model refinement.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anions / chemistry
  • Dimerization
  • Fluorescence Resonance Energy Transfer
  • Islet Amyloid Polypeptide / chemistry*
  • Nanostructures / chemistry
  • Protein Structure, Secondary
  • Rats

Substances

  • Anions
  • Islet Amyloid Polypeptide