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Fluorescent Probing of Urea‐induced Chemical Unfolding of Bovine Serum Albumin by Intramolecular Charge Transfer Fluorescence Probe E‐3‐(4‐Dimethylamino‐Naphthalen‐1‐yl)‐Acrylic Acid
Author(s) -
Ghosh Shalini,
Guchhait Nikhil
Publication year - 2010
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.2009.00665.x
Subject(s) - chemistry , fluorescence , bovine serum albumin , quenching (fluorescence) , polarity (international relations) , fluorescence spectroscopy , denaturation (fissile materials) , urea , photochemistry , acrylic acid , intramolecular force , acrylamide , solvent , biophysics , analytical chemistry (journal) , chromatography , nuclear chemistry , stereochemistry , biochemistry , organic chemistry , physics , monomer , quantum mechanics , biology , copolymer , cell , polymer
Changes in polarity at the immediate binding site in protein bovine serum albumin (BSA) produces distinct changes in the solvent polarity‐dependent emission band of fluorescence probe E‐3‐(4‐dimethylamino‐naphthalen‐1‐yl)‐acrylic acid. Steady‐state spectroscopy and time‐resolved spectroscopy have been used to investigate this binding process. Attaching the probe to BSA and then monitoring its spectral changes with increasing urea concentration and raising temperature has also tracked the denaturation of BSA chemically and thermally. The polarity of the microenvironment was investigated employing the Reichardt E T (30) scale. Fluorescence anisotropy, red edge excitation shifts and acrylamide‐induced quenching of fluorescence have been exploited to gain better insight into this binding process.