2013; Chemical and Biological Sciences 47 (1 (230): 50–53
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INFLUENCE OF DIMETHYLSULFOXIDE ON THE FLUORESCENCE BEHAVIOR OF HUMAN SERUM ALBUMIN STUDIED BY EXCITATIONEMISSION MATRIX FLUORESCENCE SPECTROSCOPY METHOD

K.R. Grigoryan*

Received: 2025-03-12 · Published: 2013-03-10

© 2013 The Author(s) and the original publisher.

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Original title
INFLUENCE OF DIMETHYLSULFOXIDE ON THE FLUORESCENCE BEHAVIOR OF HUMAN SERUM ALBUMIN STUDIED BY EXCITATIONEMISSION MATRIX FLUORESCENCE SPECTROSCOPY METHOD
Author
K.R. Grigoryan
Published
2013-03-10
Licence
as stated by the publisher

Abstract

Three-D excitation-emission matrix (EEM) fluorescence spectra of Human Serum Albumin (HSA) were measured at the presence of dimethylsulfoxide (DMSO) at t=25°C during 270 min before and after adding DMSO in different concentrations. It has been shown that DMSO at low concentrations (5%) increase heat-resistance of HSA changing the solvent structure around the protein molecule, it causes conformational changes as well in protein. Drastic changes are observed in the protein struture at DMSO higher concentration (20%). Keywords: human serum albumin, excitation-emission matrix, fluorescence spectroscopy, dimethylsulfoxide, structural changes.
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