Research Papers

Interaction of amylin species with transition metals and membranes

by Mawadda Alghrably, Iwona Czaban, Łukasz Jaremko, Mariusz Jaremko
Journal of Inorganic Biochemistry Year: 2019 DOI: 10.1016/j.jinorgbio.2018.11.004

Extra Information

Focused review


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.


Aggregation Aggregation inhibition Amylin Complex formation Diabetes type II Transition metals