Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1768, Issue 9, Pages 2026-2029Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2007.07.001
Keywords
islet amyloid polypeptide; amylin; solid-stat NMR; membrane; nanotubes
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Funding
- NIAID NIH HHS [R01 AI054515, R01 AI054515-04] Funding Source: Medline
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A key factor in the development of Type II diabetes is the loss of insulin producing pancreatic p-cells. The amyloidogenic human Islet Amyloid Polypeptide (hIAPP also known as human amylin) is believed to play a crucial role in this biological process. Previous studies have shown that WAPP forms small aggregates that kill beta-cells by disrupting the cellular membrane. In this study, we report membrane fragmentation by hIAPP using solid-state NMR experiments on nanotube arrays of anodic aluminum oxide containing aligned phospholipid membranes. In a narrow concentration range of hIAPP, an isotropic (31)p chemical shift signal indicative of the peptide-induced membrane fragmentation was detected. Solid-state NMR results suggest that membrane fragmentation is related to peptide aggregation as the presence of Congo Red, an inhibitor of amyloid formation, prevented membrane fragmentation and the non-amyloidogenic rat-IAPP did not cause membrane fragmentation. The disappearance of membrane fragmentation at higher concentrations of hIAPP suggests an alternate kinetic pathway to fibril formation in which membrane fragmentation is inhibited. (C) 2007 Elsevier B.V. All rights reserved.
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