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Updated: Jul 4, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin)
Jed J W Wiltzius1, Stuart A Sievers, Michael R Sawaya
1Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, California 90095-1570, USA.
Abstract:
Human islet amyloid polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid-like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full-length IAPP polymorph.
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