Phosphorescent probe methods in studying the interaction of glycated and non-glycated human serum albumins
Vyacheslav I. Kochubey,1 Alexander B. Pravdin,1 Andrey G. Melnikov,2 Denis A. Bykov,2 Dmitrii Baranov,2 Gennady V. Melnikov,2 1 Saratov State University, Saratov, Russia, 2 Saratov State Technical University, Saratov, Russia
Abstract
The work is devoted to the study of the processes of interaction between glycated (gHSA) and non-glycated (HSA) globules of human serum albumin. Phosphate buffer pH7.4 was chosen as the medium. The intensity and decay kinetics of the phosphorescence of the eosin fluorescent probe was sensitive to the ratio of glycated and non-glycated proteins. To explain the increase in the intensity and lifetime of eosin phosphorescence upon passing from a solution (HSA) to a mixture of HSA and gHSA, we assumed that globules of HSA and gHSA can form aggregates. The formation of such complex aggregates consisting of several protein globules leads to a decrease in the diffusion mobility of eosin, and also contributes to the screening of eosin molecules from residual oxygen dissolved in an aqueous solution, which is an effective quencher of eosin triplet states.
Speaker
Melnikov Andrey
Saratov State Technical University
Russia
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