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Rutin is an anticancer herbal drug. The interaction between rutin and bovine serum albumin (BSA) was studied by using absorption, steady-state, time resolved and synchronous fluorescence spectroscopic techniques. The results of fluorescence titration revealed that rutin could strongly quench the intrinsic fluorescence of BSA through a static quenching process. The binding constant and number of binding sites of rutin with BSA were obtained by fluorescence quenching method. The distance between donor and acceptor is calculated according to Förster's non-radiative energy transfer theory. The results of synchronous fluorescence spectra showed that the binding of rutin with BSA can induce conformational changes in BSA and it was further confirmed by docking studies. Molecular docking of rutin with BSA indicated that it docked close to Trp 212, which is present within the hydrophobic subdomain. In addition, the effect of metal ions on the binding constants of BSA⋯rutin complex has also been discussed.

Spectroscopic and Molecular Docking Investigations on the Interaction of Rutin with Bovine Serum Albumin