Journal
JOURNAL OF LUMINESCENCE
Volume 130, Issue 2, Pages 211-216Publisher
ELSEVIER
DOI: 10.1016/j.jlumin.2009.07.033
Keywords
Spectroscopy; Bovine serum albumin; Fluoxetine hydrochloride; Quenching mechanism; Thermodynamic parameters; Displacement studies
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Funding
- Council of Scientific and Industrial Research, New Delhi [01(2279)/08/EMR-II]
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The mechanism of interaction of an antidepressant, fluoxetine hydrochloride (FLX) with bovine serum albumin (BSA) has been studied by different spectroscopic techniques under physiological conditions. FLX was found to quench the intrinsic fluorescence of protein by static quenching mechanism. The binding constant 'K' was found to be 7.06 x 10(3) M-1 at 296 K. The value of 'n' close to unity revealed that the BSA has a single class of binding site for FLX. Based on thermodynamic parameters, hydrogen bonding and van der Waals forces were proposed to operate between BSA and FLX. The change in conformation of protein was noticed upon its interaction with the drug. From displacement studies it was concluded that the FLX bound to protein at site I. The effects of various common metals ions on the binding were also investigated. (C) 2009 Published by Elsevier B.V.
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