Study of the interaction between fluoxetine hydrochloride and bovine serum albumin in the imitated physiological conditions by multi-spectroscopic methods

• Published in: Journal of luminescence Vol. 130; no. 2; pp. 211 - 216
• Main Authors: Katrahalli, Umesha, Jaldappagari, Seetharamappa, Kalanur, Shankara S.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.02.2010; Elsevier
• Subjects: Biological and medical sciences; Bovine serum albumin; Displacement studies; Fluoxetine hydrochloride; Fundamental and applied biological sciences. Psychology; Interactions. Associations; Intermolecular phenomena; Molecular biophysics; Quenching mechanism; Spectroscopy; Thermodynamic parameters; Thermodynamic parameters; Spectroscopy; Bovine serum albumin; Displacement studies; Quenching mechanism; Fluoxetine hydrochloride; Fluoxetine; Albumin; Molecular interaction; Protein; Spectrometry; Thermodynamic analysis; Measurement method; Conformation
• ISSN: 0022-2313; 1872-7883
• DOI: 10.1016/j.jlumin.2009.07.033

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 7.06×10 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.