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Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance.
Atrián-Blasco, Elena; Gonzalez, Paulina; Santoro, Alice; Alies, Bruno; Faller, Peter; Hureau, Christelle.
Afiliación
  • Atrián-Blasco E; CNRS, LCC (Laboratoire de Chimie de Coordination), 205 route de Narbonne, BP 44099 31077 Toulouse Cedex 4, France.
  • Gonzalez P; University of Toulouse, UPS, INPT, 31077 Toulouse Cedex 4, France.
  • Santoro A; Biometals and Biology Chemistry, Institut de Chimie (CNRS UMR7177), Université de Strasbourg, 4 rue B. Pascal, 67081 Strasbourg, France.
  • Alies B; University of Strasbourg Institute for Advanced Study (USIAS), Strasbourg, France.
  • Faller P; Biometals and Biology Chemistry, Institut de Chimie (CNRS UMR7177), Université de Strasbourg, 4 rue B. Pascal, 67081 Strasbourg, France.
  • Hureau C; University of Strasbourg Institute for Advanced Study (USIAS), Strasbourg, France.
Coord Chem Rev ; 375: 38-55, 2018 Sep 15.
Article en En | MEDLINE | ID: mdl-30262932
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. Even more, 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-ß, α-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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Coord Chem Rev Año: 2018 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Coord Chem Rev Año: 2018 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Suiza