Copper coordination to the prion protein: Insights from theoretical studies

Article ID	Journal	Published Year	Pages	File Type
10569606	Coordination Chemistry Reviews	2013	16 Pages	PDF

Abstract

âº Theoretical studies yield important insights into the nature of Cu-PrPC interactions. âº The dominant Cu(II) bonding interactions involve deprotonated amides. âº The electronic structure of each Cu binding mode influences its redox properties. âº Key factors determining the direction of Cu binding to the backbone are discussed. âº The potential impact of Cu-PrPC interactions in protein folding is discussed.

Keywords

PBE CJD TSE GPi N-methyl-d-aspartate NMDA MAD B3LYP ENDOR LMCT Car–Parrinello molecular dynamics GTO PW91 CPMD ESEEM PrPc NHE BP86 BSE PrPsc scrapie prion protein ESI Slater type orbitals STO nuclear magnetic resonance GGA DFT QM/MM ROS UV–visible Ascorbic acid Ultraviolet–visible normal hydrogen electrode Ligand to metal charge transfer Transmissible spongiform encephalopathies Creutzfeldt–Jakob disease LDA NMR EPR Electron paramagnetic resonance Generalized gradient approximation Local density approximation Molecular dynamics Electron nuclear double resonance circular dichroism electronic structure SOD Superoxide dismutase Coordination chemistry Electron spin echo envelope modulation Copper Quantum mechanics/molecular mechanics Mean absolute deviation Density functional theory Prion protein cellular prion protein glycosyl-phosphatidylinositol Reactive oxygen species electrospray ionization