Interaction of amylin species with transition metals and membranes
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Online Publication Date2018-11-10
Print Publication Date2019-02
Permanent link to this recordhttp://hdl.handle.net/10754/629864
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AbstractIslet Amyloid Polypeptide (IAPP), also known as amylin, is a 37-amino-acid peptide hormone that is secreted by pancreatic islet β-cells. Amylin is complementary to insulin in regulating and maintaining blood glucose levels in the human body. The misfolding and aggregation of amylin is primarily associated with type 2 diabetes mellitus, which is classified as an amyloid disease. Recently, the interactions between amylin and specific metal ions, e.g., copper(II), zinc(II), and iron(II), were found to impact its performance and aggregation processes. Therefore, the focus in this review will be on how the chemistry and structural properties of amylin are affected by these interactions. In addition, the impact of amylin and other amyloidogenic peptides interacting with metal ions on the cell membranes is discussed. In particular, recent studies on the interactions of amylin with copper, zinc, iron, nickel, gold, ruthenium, and vanadium are discussed.
CitationAlghrably M, Jaremko Ł, Czaban I, Jaremko M (2018) Interaction of amylin species with transition metals and membranes. Journal of Inorganic Biochemistry. Available: http://dx.doi.org/10.1016/j.jinorgbio.2018.11.004.
SponsorsAuthors would like to thank King Abdullah University of Science and Technology (KAUST) for financial support.