Interaction of amylin species with transition metals and membranes

Mawadda Alghrably, Iwona Czaban, Lukasz Jaremko, Mariusz Jaremko

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

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.
Original languageEnglish (US)
Pages (from-to)69-76
Number of pages8
JournalJournal of Inorganic Biochemistry
Volume191
DOIs
StatePublished - Nov 10 2018

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