Spectroscopic and Molecular Docking Investigations on the Interaction of Rutin with Bovine Serum Albumin
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M. Asha Jhonsi
Abstract
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.
© by Oldenbourg Wissenschaftsverlag, Tiruchirappalli 620024, Tamil Nadu, Germany
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Articles in the same Issue
- Highly Ordered 3D-Macroporous Poly(Para-Phenylene) Films Made by Electropolymerization of Benzene in an Ionic Liquid
- Oscillations of a Hanging Liquid Drop, Driven by Interfacial Dielectric Force
- Phase Behaviour of CoCl2-MnCl2 Mixed Crystals
- Isentropic Compressibility Studies of Some Salts in Acetonitrile + N,N-dimethylacetamide Mixtures at 298 K
- Solubility Enhancement of Polycyclic Aromatic Hydrocarbons (PAHs) Using Synergistically Interacting Gemini-Conventional Surfactant Systems
- Spectroscopic and Molecular Docking Investigations on the Interaction of Rutin with Bovine Serum Albumin
- Spectroscopic Studies on the Interaction of Synthetic Food Colorants with Bovine Serum Albumin
