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Interactions driving the collapse of islet amyloid polypeptide: implications for amyloid aggregation


Abstract Human islet amyloid polypeptide (hIAPP), also known as amylin, is a 37-residue intrinsically disordered hormone involved in glucose regulation and gastric emptying. The aggregation of hIAPP into amyloid fibrils is believed to play a causal role in type 2 diabetes. To date, not much is known about the monomeric state of hIAPP or how it undergoes an irreversible transformation from disordered peptide to insoluble aggregate. IAPP contains a highly conserved disulfide bond that restricts hIAPP(1-8) into a short ring-like structure: N_loop. Removal or chemical reduction of N_loop not only prevents cell response upon binding to the CGRP receptor, but also alters the mass per length distribution of hIAPP fibers and the kinetics of fibril formation... (more)
Created Date 2013
Contributor Cope, Stephanie M. (Author) / Vaiana, Sara M (Advisor) / Ghirlanda, Giovanna (Committee member) / Ros, Robert (Committee member) / Lindsay, Stuart M (Committee member) / Ozkan, Sefika B (Committee member) / Arizona State University (Publisher)
Subject Biophysics / Physics / amylin / amyloid aggregation / islet amyloid polypeptide / N_loop / proline
Type Doctoral Dissertation
Extent 137 pages
Language English
Copyright
Reuse Permissions All Rights Reserved
Note Ph.D. Physics 2013
Collaborating Institutions Graduate College / ASU Library
Additional Formats MODS / OAI Dublin Core / RIS


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Description Dissertation/Thesis