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

Thibaut Galler¹, Vincent Lebrun¹, Laurent Raibaut¹

¹Institut de Chimie, UMR 7177, CNRS-Universitéde Strasbourg, 4 rue Blaise Pascal, Strasbourg 67000, France. pfaller@unistra.fr.

Chemical Communications (Cambridge, England)

|September 11, 2020

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.

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