Abstract
Abstract The interaction between isatin moiety 2-amino-3-cyano-5-bromospiro (5H-indeno [1, 2-b] pyran-4,3′indoline)-2′5,‑dione (ACBSIPID) and bovine serum albumin (BSA) has been interpret under physiological conditions using fluorescence, circular dichroism and molecular docking studies. The formation of ACBSIPID-BSA complex leading to the fluorescence quenching of BSAwas evaluated by spectrofluorimetry. The mechanism for fluorescence diminishing and mode of binding was investigated by temperature effect. Furthermore, the quenching assessed by time-resolved fluorescence study, result confirmed the static nature of quenching. Whereas the binding distance (r) between ACBSIPID and BSA was found to be 3.12 nm by Forster's theory of nonradiative energy transfers. Based on CD spectra, it was observed that the presence of ACBSIPID decreased the α-helical content of BSA and induced unfolding of a polypeptide chain of the protein. The molecular docking study indicates ACBSIPID drug having plausible binding affinity towards the BSA complex enzyme.
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