Article ID Journal Published Year Pages File Type
1231500 Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2013 10 Pages PDF
Abstract

The interaction of genistein with bovine serum albumin (BSA) has been characterized via UV–vis, fluorescence spectroscopy and Circular Dichroism (CD) measurements under physiological conditions. In this study, we have investigated the effect of some common metal ions on the binding of genistein with BSA using fluorescence studies. The fluorescence data reveal that the binding affinity of genistein to BSA increases in presence of certain metal ions. The possibility of non-radiative energy transition from the donor tryptophan to the acceptor genistein has been observed in absence and presence of metal ions. The observed similarities in the values of efficiency of energy transfer (E) and the separation between the donor and acceptor (r) in both the cases may be correlated with the complexation between the genistein and metal ions, which is also observed from the UV–vis studies. The changes in enthalpy (ΔH°) and entropy (ΔS°) of the interaction were found to be −14.64 kJ mol−1 and +42.75 J mol−1 K−1 respectively. These values indicate the involvement of electrostatic interactions along with a hydrophobic association that results in a positive entropy change. CD analysis shows that there is a slight increase in the% α-helical content of BSA on binding with genistein at lower molar ratios. Warfarin and ibuprofen displacement studies in accordance with the molecular docking show that genistein binds to site I (subdomain IIA) of BSA.

Graphical abstractGenistein binds near to Trp 213 (subdomain IIA, site 1) of bovine serum albumin.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Genistein binds to hydrophobic pocket (site 1, subdomain IIA) of BSA. ► Binding mainly occurs via hydrophobic interactions. ► Negative values of ΔG° indicate the spontaneity of binding. ► Presences of metal ions affect the binding of genistein with BSA. ► Non-radiative energy transfer occurs from donor tryptophan to acceptor genistein.

Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
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