Interaction of amylin species with transition metals and membranes
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Type
ArticleKAUST Department
Biological and Environmental Sciences and Engineering (BESE) DivisionBioscience Program
Date
2018-11-10Online Publication Date
2018-11-10Print Publication Date
2019-02Permanent link to this record
http://hdl.handle.net/10754/629864
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Islet 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.Citation
Alghrably 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.Sponsors
Authors would like to thank King Abdullah University of Science and Technology (KAUST) for financial support.Publisher
Elsevier BVAdditional Links
https://www.sciencedirect.com/science/article/pii/S0162013418304409ae974a485f413a2113503eed53cd6c53
10.1016/j.jinorgbio.2018.11.004