Chemistry

Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix

Document Type

Article

Abstract

Understanding how small molecules affect amyloid formation is of major biomedical and pharmaceutical importance due to the association of amyloid with incurable diseases including Alzheimer's, Parkinson's, and type II diabetes. Using solution state 1H NMR, we demonstrate that curcumin, a planar biphenolic compound found in the Indian spice turmeric, delays the self-assembly of islet amyloid polypeptide to NMR-invisible assemblies. Accompanying circular dichroism studies show that curcumin disassembles α-helix in maturing assemblies of IAPP. The amount of α-helix disassembled correlates with predicted and experimentally determined helical content of IAPP obtained by others. Taken together, these results indicate that curcumin modulates IAPP self-assembly by unfolding α-helix on pathway to amyloid. The implications of this work in the elucidation of the mechanism for amyloid formation by IAPP in the presence of curcumin are discussed. © 2012 Elsevier Inc..

Publication Title

Biochemical and Biophysical Research Communications

Publication Date

6-15-2012

Volume

422

Issue

4

First Page

551

Last Page

555

ISSN

0006-291X

DOI

10.1016/j.bbrc.2012.05.013

Keywords

Amyloid, Amyloid formation, Curcumin, Inhibitors of amyloid

Cross Post Location

Student Publications

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