Chemical communications

Abstract

Employing peptide-based models of copper transporter 1 (CTR1), we show that the trimeric arrangement of its N-terminus tunes its reactivity with Cu, promoting Cu(II) reduction and stabilizing Cu(I). Hence, the employed multimeric models of CTR1 provide an important contribution to studies on early steps of Cu uptake by cells.

 

Reference

How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry
Thibaut Galler, Vincent Lebrun, Laurent Raibaut, Peter Faller* and Nina E. Wezynfeld
Chemical communications, First published : 2 September 2020 – DOI :https://doi.org/10.1039/D0CC04693K

 

Contact

Thibaut Galler, Nina wezynfeld & Peter Faller, équipe BCB, Institut de Chimie (UMR 7177).

Université de Strasbourg
Centre national de la recherche scientifique | CNRS
Fondation Jean-Marie Lehn