Journal article
Structural Insight into Redox Dynamics of Copper Bound N-Truncated Amyloid-β Peptides from in Situ X-ray Absorption Spectroscopy
VA Streltsov, RSK Ekanayake, SC Drew, CT Chantler, SP Best
Inorganic Chemistry | AMER CHEMICAL SOC | Published : 2018
Abstract
X-ray absorption spectroscopy of CuII amyloid-β peptide (Aβ) under in situ electrochemical control (XAS-EC) has allowed elucidation of the redox properties of CuII bound to truncated peptide forms. The Cu binding environment is significantly different for the Aβ1-16 and the N-truncated Aβ4-9, Aβ4-12, and Aβ4-16 (Aβ4-9/12/16) peptides, where the N-truncated sequence (F4R5H6) provides the high-affinity amino-terminal copper nickel (ATCUN) binding motif. Low temperature (ca. 10 K) XAS measurements show the adoption of identical CuII ATCUN-type binding sites (CuII ATCUN) by the first three amino acids (FRH) and a longer-range interaction modeled as an oxygen donor ligand, most likely water, to g..
View full abstractGrants
Funding Acknowledgements
We would like to acknowledge that this research was undertaken with support of the XAS beamline scientists at the Australian Synchrotron, Victoria, Australia. We would like to thank Mariuz Mital for help in preparation of samples. R.S.K.E. was supported by The Laby Foundation scholarship awarded by The School of Physics, The University of Melbourne. S.C.D. was supported by a research fellowship awarded by the faculty of Medicine, Dentistry and Health Sciences, The University of Melbourne.