A method of fluorescence polarization of probes in the study of the interaction of glycated serum albumin with non-glycated one
Andrei G. Melnikov1; Alexander B. Pravdin2; 1Saratov State Technical University, Saratov, Russia; 2Saratov State University, Saratov, Russia
Abstract
Polarization fluorescence spectroscopy was used to study the interaction of the fluorescent probe eosin Y with glycated and native proteins - human serum albumin (HSA). Fluorescence and absorption spectroscopy revealed that eosin effectively binds to glycated proteins (gHSA) and non-glycated (native) HSA globules. It was found that upon transition from HSA to glycated gHSA, a decrease in the fluorescence intensity of the probe (eosin) bound to the protein globules was observed.
This result can be explained by changes in the microenvironment of eosin localized within the gHSA globule. In a mixture of glycated and non-glycated proteins, an increase in eosin fluorescence intensity was observed compared to HSA solutions. A study of eosin fluorescence polarization in solutions of HSA, gHSA, and a 1:1 mixture of HSA and gHSA revealed that the maximum anisotropy is achieved in the HSA and gHSA mixture. This is hypothesized to be due to the formation of a complex consisting of HSA and gHSA globules.
Speaker
Melnikov Andrei Gennadievich
Saratov State Technical University, Associated professor at Physics Department
Russia
Discussion
Ask question
