ATOMIC STRUCTURE OF THE CROSS-BETA SPINE OF ISLET AMYLOID POLYPEPTIDE (AMYLIN)

$20,721P41FY2009RRNIH

Cornell University, Ithaca NY

Investigators

Linked publications & trials

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Abstract

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. 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. The goal of this subproject is to find the structure of the fibrillar form of IAPP and to understand how the IAPP peptide forms fibrillar deposits in the pancreas.

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