Solvation effects in human serum albumin radiolysis in the presence of dimethyl sulfoxide

PMR and electrophoresis have been applied to examine hydration changes in protein molecules due to the presence of the electron donor dimethylsulfoxide DMSO, which influences the radiolysis of human serum albumin HSA. The reactions of aqueous HSA with added DMSO show that the DMSO on the one hand acts as a protector, which prevents the formation of low-molecular protein forms on reaction with hydroxyl radicals, and on the other alters the protein hydration, which facilitates thiol-di-sulfide exchange, which leads to oligomers.Translated from Teoreticheskaya i Éksperimental'naya Khimiya, Vol. 26, No. 1, pp. 107–111, January–February, 1990.