Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance

被引：139
作者：
Atrian-Blasco, Elena [1 ,2 ]
Gonzalez, Paulina [3 ,4 ]
Santoro, Alice [3 ,4 ]
Alies, Bruno [5 ]
Faller, Peter [3 ,4 ]
Hureau, Christelle [1 ,2 ]
机构：
[1] CNRS, LCC, 205 Route Narbonne,BP 44099, F-31077 Toulouse 4, France
[2] Univ Toulouse, UPS, INPT, F-31077 Toulouse 4, France
[3] Univ Strasbourg, CNRS, UMR7177, Biomet & Biol Chem,Inst Chim, 4 Rue B Pascal, F-67081 Strasbourg, France
[4] Univ Strasbourg, Inst Adv Study USIAS, Strasbourg, France
[5] Univ Bordeaux, ChemBioPharm, INSERM, CNRS,U1212,UMR 5320, Bordeaux, France
来源：
COORDINATION CHEMISTRY REVIEWS | 2018年 / 371卷
关键词：
Amyloid-beta; alpha-Synuclein; Amylin; Familial mutations; Copper; Zinc; N-TERMINAL ACETYLATION; A-BETA PEPTIDE; ALPHA-SYNUCLEIN AGGREGATION; METAL-CATALYZED OXIDATION; CU(II) BINDING-SITES; ALZHEIMERS-DISEASE; BIOINORGANIC CHEMISTRY; COPPER-BINDING; IN-VITRO; ZINC-BINDING;
D O I：
10.1016/j.ccr.2018.04.007
中图分类号：
O61 [无机化学];
学科分类号：
070301 ; 081704 ;
摘要：
Several diseases share misfolding of different peptides and proteins as a key feature for their development. This is the case of important neurodegenerative diseases such as Alzheimer's and Parkinson's diseases and type II diabetes mellitus. Furthermore, metal ions such as copper and zinc might play an important role upon interaction with amyloidogenic peptides and proteins, which could impact their aggregation and toxicity abilities. In this review, the different coordination modes proposed for copper and zinc with amyloid-beta, alpha-synuclein and IAPP will be reviewed as well as their impact on the aggregation, and ROS production in the case of copper. In addition, a special focus will be given to the mutations that affect metal binding and lead to familial cases of the diseases. Different modifications of the peptides that have been observed in vivo and could be relevant for the coordination of metal ions are also described. (C) 2018 Elsevier B.V. All rights reserved.
引用
收藏
页码：38 / 55
页数：18
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