Fluorescent eosin probe in investigations of structural changes in glycated proteins

The possibility of using the luminescent-kinetic probe method to investigate structural changes in bovine serum albumin (BSA) upon nonenzymatic thermal glycation is studied. An increase in the glycation time lead to a decrease in the intensity of the probe (eosin) fluorescence and to a long-waveleng...

Full description

Saved in:
Bibliographic Details
Published in:Optics and spectroscopy 2010-08, Vol.109 (2), p.193-196
Main Authors: Pravdin, A. B., Kochubey, V. I., Mel’nikov, A. G.
Format: Article
Language:English
Subjects:
Biomedical Optics and Spectroscopy
Lasers
Optical Devices
Optics
Photonics
Physics
Physics and Astronomy
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The possibility of using the luminescent-kinetic probe method to investigate structural changes in bovine serum albumin (BSA) upon nonenzymatic thermal glycation is studied. An increase in the glycation time lead to a decrease in the intensity of the probe (eosin) fluorescence and to a long-wavelength shift of its maximum, as well as to an increase in the eosin phosphorescence intensity, which indicates that eosin binds to hydrophobic regions of protein at any times of incubation of BSA with glucose. From a decrease in the rate constant of the triplet-triplet energy transfer between the donor (eosin) and acceptor (anthracene) bound to proteins, it is found that the changes observed in the spectral characteristics of eosin are caused by structural changes in albumin globules as a result of glycosylation.
ISSN:0030-400X
1562-6911
DOI:10.1134/S0030400X10080072