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|Title:||Investigations on interaction between atazanvir sulphate and bovine serum albumin by fluorescence spectroscopy|
|Authors:||Mote, Umesh S|
Kolekar, G B
|Keywords:||Fluorescence quenching;Thermodynamic parameters;Synchronous fluorescence;Binding constant|
|Abstract:||The interaction between bovine serum albumin (BSA) and atazanvir sulphate (AS) has been investigated under the physiological pH 7.4 condition using fluoresence spectroscopy. The binding constant, number of binding site, thermodynamic parameters such as ∆G, ∆H, ∆S and nature of binding forces between BSA-AS have been obtained from the steady state fluorescence quenching of BSA by AS. The static quenching is confirmed from Stern-Volmer quenching constant at different temperatures. The effect of AS on the conformation of BSA has been analyzed using synchronous and three-dimensional fluorescence spectroscopy.|
|Appears in Collections:||IJC-A Vol.55A(07) [July 2016]|
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