Title : A Novel SOD1 Intermediate Oligomer, Role of Free Thiols and Disulfide Exchange.

Pub. Date : 2020

PMID : 33679289






4 Functional Relationships(s)
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1 A Novel SOD1 Intermediate Oligomer, Role of Free Thiols and Disulfide Exchange. Disulfides superoxide dismutase 1 Homo sapiens
2 Wild-type human SOD1 forms a highly conserved intra-molecular disulfide bond between C57-C146, and in its native state is greatly stabilized by binding one copper and one zinc atom per monomer rendering the protein dimeric. Disulfides superoxide dismutase 1 Homo sapiens
3 Here we further investigate the role of reduction of the native C57-C146 disulfide bond in fibrillation of wild-type hSOD1, firstly through removal of free thiols by paired mutations C6A, C111S (AS-SOD1), and secondly in seeded fibrillation reactions modulated by reductant tris (2-carboxyethyl) phosphine (TCEP). Disulfides superoxide dismutase 1 Homo sapiens
4 Fibrillation of AS-SOD1 was dependent upon disulfide reduction and showed classic lag and exponential growth phases compared with wild-type hSOD1 whose fibrillation trajectories were typically somewhat perturbed. Disulfides superoxide dismutase 1 Homo sapiens