Binding of fexofenadine hydrochloride to bovine serum albumin: structural considerations by spectroscopic techniques and molecular docking.
The binding interaction of peripheral H1receptor antagonist drug, fexofenadine hydrochloride to bovine serum albumin (BSA) is investigated by fluorescence spectroscopy in combination with UV-absorption spectroscopy under physiological conditions. The Stern-Volmer plots at different temperatures and the steady state fluorescence suggested a static type of interaction between fexofenadine and BSA. Binding constants were determined to provide a measure of the binding affinity between fexofenadine and BSA. It was found that BSA has one binding site for fexofenadine. On the basis of the competitive site marker experiments and thermodynamic results, it was considered that fexofenadine was primarily bound to the site I of BSA mainly by hydrogen bond and van der Waals force. Utilising Förster resonance energy transfer the distance, r between the donor, BSA and acceptor fexofenadine was obtained. Furthermore, the results of circular dichroism and synchronous fluorescence spectrum indicated that the secondary structure of BSA was changed in the presence of fexofenadine. Molecular docking was applied to further define the interaction of fexofenadine with BSA.
a P.G. Department of Studies in Chemistry , Karnatak University , Dharwad 580 003 , India.
Laxmi N
LN
Jattinagoudar
a P.G. Department of Studies in Chemistry , Karnatak University , Dharwad 580 003 , India.
Sharanappa T
ST
Nandibewoor
a P.G. Department of Studies in Chemistry , Karnatak University , Dharwad 580 003 , India.
Shivamurti A
SA
Chimatadar
D000818:Animals; D001665:Binding Sites; D008968:Molecular Conformation; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013057:Spectrum Analysis / Q000379:methods; D016593:Terfenadine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics
D012710:Serum Albumin, Bovine; D016593:Terfenadine; C093230:fexofenadine
bovine serum albumin; conformational change; energy transfer; fexofenadine hydrochloride; molecular docking