Journal article
The N-terminal 14-mer model peptide of human Ctr1 can collect Cu(ii) from albumin. Implications for copper uptake by Ctr1
E Stefaniak, D Płonka, SC Drew, K Bossak-Ahmad, KL Haas, MJ Pushie, P Faller, NE Wezynfeld, W Bal
Metallomics | ROYAL SOC CHEMISTRY | Published : 2018
DOI: 10.1039/c8mt00274f
Abstract
Human cells acquire copper primarily via the copper transporter 1 protein, hCtr1. We demonstrate that at extracellular pH 7.4 Cu II is bound to the model peptide hCtr1 1-14 via an ATCUN motif and such complexes are strong enough to collect Cu II from albumin, supporting the potential physiological role of Cu II binding to hCtr1.
Grants
Awarded by National Institutes of Health
Funding Acknowledgements
The equipment used was sponsored in part by the Centre for Preclinical Research and Technology (CePT), a project co-sponsored by European Regional Development Fund and Innovative Economy, The National Cohesion Strategy of Poland. The study was financed by the Preludium grant, No. 2016/21/N/NZ1/02785, by Opus grant No. 2016/23/B/ST5/02253, National Science Centre of Poland, and by the Frontier Research in Chemistry Foundation, Strasbourg (CSC-PFA-17). N.E. Wezynfeld was supported by Start Programme funded by Polish Science No. START 90.2017 and Mobility Plus Programme funded by Polish Ministry of Science and Higher Education No. 1632/MOB/V/2017/0. K.H. gratefully acknowledges support from a Research Corporation for Science Advancement Cottrell Scholar Award (No. 23666). Portions of this research were carried out at the Stanford Synchrotron Radiation Lightsource, a Directorate of SLAC National Accelerator Laboratory and an Office of Science User Facility operated for the U.S. Department of Energy Office of Science by Stanford University. The SSRL Structural Molecular Biology Program is supported by the DOE Office of Biological and Environmental Research, and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program (P41RR001209).