albumin - publications

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Docking investigation and binding interaction of benzimidazole derivative with bovine serum albumin.

J Photochem Photobiol B. 2012 Sep 5;117C:27-32

Authors: Jayabharathi J, Jayamoorthy K, Thanikachalam V


(1)H NMR, (13)C NMR and Mass spectral analysis have been made for 1-(4-fluorobenzyl)-2-(4-fluorophenyl)-1H-benzo[d]imidazole (FBFPB). The mutual interaction of FBFPB with bovine serum albumin (BSA) was investigated using absorption, fluorescence and synchronous fluorescence spectral studies. The binding distance has been determined based on the theory of Forester's non-radiation energy transfer (FRET). The calculated quenching constants (K(sv)) were 2.84×10(4), 2.55×10(4) and 2.37×10(4) at 301, 310 and 318K respectively. The Stern-Volmer quenching constant (K(sv)), binding site number (n), apparent binding constant (K(A)) and corresponding thermodynamic parameters (ΔG, ΔH and ΔS) were calculated. The interaction between FBFPB and BSA have discussed by molecular docking technique.

PMID: 23026385 [PubMed - as supplied by publisher]