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

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• 作者：Samuel Sparks ; Gai Liu ; Kevin J. Robbins ; Noel D. Lazo ; ^{nlazo@clarku.edu}
• 关键词：Amyloid ; Amyloid formation ; Inhibitors of amyloid ; Curcumin
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2012
• 期刊代码：159_0006291x
• 类别：bio
• 出版时间：15 June, 2012
• 卷：422
• 期：4
• 页码：551-555
• 文件大小：507 K

摘要

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鈥檚, Parkinson鈥檚, 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 伪-helix in maturing assemblies of IAPP. The amount of 伪-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 伪-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.