Electron excitation energy transfer spectroscopy in the study of structural changes in glycated transport proteins.

Abstract

The processes of interaction between glycated and non-glycated human serum albumin (HSA) proteins were investigated using the method of singlet-singlet energy transfer occurring via an inductive-resonance mechanism. Analysis of the fluorescence spectra of tryptophanyl residues and the absorption spectra of eosin demonstrated that energy transfer occurs between the tryptophanyl residue of HSA (as the energy donor) and the acceptor, which is the nanomarker eosin. Using absorption and fluorescence spectroscopy methods, it was established that eosin is non-covalently bound to the protein globule and is localized near the non-polar region of the protein. Based on the experimental results and in accordance with the quantum-mechanical Förster theory, the critical radii for energy transfer were determined. It was shown that the energy transfer takes place within the protein globule. The increase in the energy transfer radius value upon transitioning to glycated proteins indicates structural changes in the globule of glycated proteins compared to non-glycated ones. This assumption is supported by the results of our previous studies conducted using polarization spectroscopy methods. The obtained results may be in demand for the development of methods for early diagnosis of diabetes mellitus, as well as a number of other diseases associated with structural changes in human blood plasma transport proteins.

Speaker

Alexander Romanovich Milkin
Yuri Gagarin State Technical University of Saratov
Russia

Discussion

Ask question