Issue 81, 2020

How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry

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.

Graphical abstract: How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry

Supplementary files

Article information

Article type
Communication
Submitted
07 Jul 2020
Accepted
02 Sep 2020
First published
07 Sep 2020
This article is Open Access
Creative Commons BY license

Chem. Commun., 2020,56, 12194-12197

How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry

T. Galler, V. Lebrun, L. Raibaut, P. Faller and N. E. Wezynfeld, Chem. Commun., 2020, 56, 12194 DOI: 10.1039/D0CC04693K

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