Differential copper binding to alpha-synuclein and its disease-associated mutants affect the aggregation and amyloid formation

• Published in: Biochimica et biophysica acta. General subjects Vol. 1861; no. 2; pp. 365 - 374
• Main Authors: Ranjan, Priyatosh, Ghosh, Dhiman, Yarramala, Deepthi S., Das, Subhadeep, Maji, Samir K., Kumar, Ashutosh
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.02.2017
• Subjects: alpha-Synuclein - metabolism; amyloid; Amyloid - metabolism; Amyloidogenic Proteins - metabolism; Amyloidosis - metabolism; Amyloidosis - pathology; Binding Sites; Cell Line; central nervous system; Copper; Copper - metabolism; enzymes; fluorescence; homeostasis; Humans; Kinetics; Long-range contacts; mutants; Non-amyloid-β component; nuclear magnetic resonance spectroscopy; Parkinson disease; Parkinson Disease - metabolism; Parkinson Disease - pathology; Protein Aggregation, Pathological - metabolism; Protein Aggregation, Pathological - pathology; α-Syn G51D; α-Syn H50Q; α-Syn G51D; Long-range contacts; Non-amyloid-β component; Copper; α-Syn H50Q

Copper is an essential trace element required for the proper functioning of various enzymes present in the central nervous system. An imbalance in the copper homeostasis results in the pathology of various neurodegenerative disorders including Parkinson’s Disease. Hence, residue specific interaction...