The present research focuses on the binding interaction of sulfadoxine with bovine serum albumin using spectrofluorimetry under simulated physiological conditions. During the course of the research, various spectroscopic and other techniques such as Raman, CD, lifetime measurement and molecular modelling were also used. It was noticeable that the intrinsic fluorescence of BSA was quenched by sulfadoxine through static quenching. The spectral and docking studies explored the change in the secondary structure of the BSA and the binding mechanism.
Author (s) DetailsDr. Jyoti Bagalkoti
P. G. Department of studies in Chemistry, Karnatak University, Dharwad-580003, Karnataka, India.
Dr. Sharanappa T. Nandibewoor
P. G. Department of studies in Chemistry, Karnatak University, Dharwad-580003, Karnataka, India.
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