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Antioxidant benzimidazole bind bovine serum albumin

Paper ID Volume ID Publish Year Pages File Format Full-Text
29510 44415 2012 8 PDF Available
Antioxidant benzimidazole bind bovine serum albumin

1-(4-Methoxybenzyl)-2-(4-methoxyphenyl)-1H-benzo[d]imidazole (MBMPB) was synthesized and characterized by 1H NMR, 13C 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 (Ksv) were calculated at different temperature. The binding site (n), apparent binding constant (KA) 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.

Graphical abstract.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Quenching mechanism mainly arise from the formation of BSA–MBMPB complex. ► The D → A distance the energy transfer from BSA to MBMPB. ► Synchronous fluorescence spectra to exploit the structural change of BSA. ► MBMPB shows potential antioxidant property.

Antioxidant; Benzimidazole; BSA; Quenching; FRET
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Antioxidant benzimidazole bind bovine serum albumin
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 115, 3 October 2012, Pages 85–92
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Physical Sciences and Engineering Chemical Engineering Bioengineering