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

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. Trimeric arrangement of model peptides of the CTR1 N-terminus promotes Cu( ii ) reduction and Cu( i ) binding.