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Journal of Diabetes Research
Volume 2015 (2015), Article ID 515307, 13 pages
Review Article

Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis

1Department of Chemistry, Pharmaqam, University of Quebec in Montreal, Montreal, QC, Canada H3C 3P8
2Quebec Network for Research on Protein Function, Structure, and Engineering (PROTEO), Canada
3Biophysics Unit (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country, 48080 Bilbao, Spain

Received 5 November 2014; Revised 26 January 2015; Accepted 9 February 2015

Academic Editor: Ehud Gazit

Copyright © 2015 Phuong Trang Nguyen et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Type II diabetes mellitus is associated with the deposition of fibrillar aggregates in pancreatic islets. The major protein component of islet amyloids is the glucomodulatory hormone islet amyloid polypeptide (IAPP). Islet amyloid fibrils are virtually always associated with several biomolecules, including apolipoprotein E, metals, glycosaminoglycans, and various lipids. IAPP amyloidogenesis has been originally perceived as a self-assembly homogeneous process in which the inherent aggregation propensity of the peptide and its local concentration constitute the major driving forces to fibrillization. However, over the last two decades, numerous studies have shown a prominent role of amyloid cofactors in IAPP fibrillogenesis associated with the etiology of type II diabetes. It is increasingly evident that the biochemical microenvironment in which IAPP amyloid formation occurs and the interactions of the polypeptide with various biomolecules not only modulate the rate and extent of aggregation, but could also remodel the amyloidogenesis process as well as the structure, toxicity, and stability of the resulting fibrils.