Interaction of amylin species with transition metals and membranes

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. Misfolded proteins can undergo fibril formation, resulting into the oligomers creation. Fe(II), Cu(II), and Zn(II) ions promote this formation. Ru, V, and some Au(III) complexes inhibit it. The effect of Au(III) complexes depend on their concentration. The role of metal ions in amyloid pore formation still needs to be investigated. [Display omitted] •Interactions of metal ions with amylin affect its structural properties.•Fe, Cu, and Zn ions promote amylin oligomers formation.•Ru, V, and some of the Au complexes inhibit it.•A case reported that the effect of Au complexes on fibril formation depends on their concentration.•The role of the metal ions in the amyloid pore formation still needs to be investigated.