Interaction of amylin species with transition metals and membranes

被引：51

作者：

Alghrably, Mawadda ^{[1
]}

Czaban, Iwona ^{[1
]}

Jaremko, Lukasz ^{[1
]}

Jaremko, Mariusz ^{[1
]}

机构：

[1] KAUST, BESE, Thuwal 239556900, Saudi Arabia

来源：

JOURNAL OF INORGANIC BIOCHEMISTRY | 2019年 / 191卷

关键词：

Diabetes type II; Transition metals; Amylin; Aggregation; Aggregation inhibition; Complex formation; ISLET AMYLOID POLYPEPTIDE; GENOME-WIDE ASSOCIATION; FIBRIL FORMATION; PANCREATIC-ISLETS; RUTHENIUM COMPLEXES; COPPER(II) COMPLEXES; ZINC SUPPLEMENTATION; ALZHEIMERS-DISEASE; HYDROGEN-PEROXIDE; OXIDATIVE STRESS;

D O I：

10.1016/j.jinorgbio.2018.11.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Islet Amyloid Polypeptide (IAPP), also known as amylin, is a 37-amino-acid peptide hormone that is secreted by pancreatic islet beta-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.

引用

页码：69 / 76

页数：8

共 95 条

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