Studies of complexes consisting of glycated and native human serum albumin proteins by polarization spectroscopy
Vyacheslav Kochubey, 1 Alexander Pravdin, 1 Denis Bykov, 2 Andrei Melnikov, 2 Gennady Melnikov, 2 1 Saratov State University, Russia 2 Saratov State Technical University, Russia
Abstract
The work is devoted to the study of the interaction of glycated human serum albumin (gHSA) with non-glycated (HAS) by the method of polarization spectroscopy. The aim of the work was to determine changes in the polarization characteristics in the luminescence spectra of the eosin probe associated with HSA and gHSA in aqueous solutions of the phosphate buffer pH7.4, which do not contain free glucose. It was found that the anisotropy of eosin fluorescence increases with the transition to solutions containing glycated proteins. It is assumed that this is due to a more rigid fixation of eosin in glycated proteins compared to non-glycated ones. An unusual dependence of the anisotropy of delayed eosin fluorescence was found when glycated gHSA was added to the HSA solution. The maximum anisotropy of delayed fluorescence occurs in a solution containing a mixture of HSA and gHSA. The results obtained can be explained by the formation of aggregates consisting of gHSA and HSA globules. The rigid fixation of eosin in such an aggregate leads to an increase in the anisotropy of delayed eosin fluorescence.
Speaker
Denis Bykov
Saratov State Technical University
Russia
Discussion
Ask question
