Binding interaction of phosphorus heterocycles with bovine serum albumin: A biochemical study.

ABSTRACT: Interaction between bovine serum albumin (BSA) and phosphorus heterocycles (PHs) was studied using multi-spectroscopic techniques. The results indicated the high binding affinity of PHs to BSA as it quenches the intrinsic fluorescence of BSA. The experimental data suggested the fluorescence quenching mechanism between PHs and BSA as a dynamic quenching. From the UV-vis studies, the apparent association constant (K_app) was found to be 9.25×10², 1.27×10⁴ and 9.01×10² L/mol for the interaction of BSA with PH-1, PH-2 and PH-3 respectively. According to the Förster's non-radiation energy transfer (FRET) theory, the binding distances between BSA and PHs were calculated. The binding distances (r) of PH-1, PH-2 and PH-3 were found to be 2.86, 3.03, and 5

SUBMITTER: Roy S 

PROVIDER: S-EPMC5686865 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature