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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
Antioxidant benzimidazole bind bovine serum albumin
J Jayabharathi1, V Thanikachalam, K Jayamoorthy
1Department of Chemistry, Annamalai University, Annamalainagar, Tamilnadu 608 002, India. jtchalam2005@yahoo.co.in
Abstract:
1-(4-Methoxybenzyl)-2-(4-methoxyphenyl)-1H-benzo[d]imidazole (MBMPB) was synthesized and characterized by (1)H NMR, (13)C NMR, Mass and IR spectral analysis. The mutual interaction of MBMPB with bovine serum albumin (BSA) was investigated using solution spectral studies. The binding distance has been calculated based on the theory of Forester's non-radiation energy transfer (FRET). The Stern-Volmer quenching constant (K(sv)) were calculated at different temperature. The binding site (n), apparent binding constant (K(A)) and corresponding thermodynamic parameters (ΔG,ΔH and ΔS) were calculated. Antioxidant analyses such as DPPH radical scavenging analysis, Superoxide anion scavenging analysis and Hydroxyl radical scavenging analysis have been carried out for MBMPB and it shows potential antioxidant property due to the presence of electron releasing methoxy group.
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