Study on the interaction of sodium morin-5-sulfonate with bovine serum albumin by spectroscopic techniques

In the present investigation, an attempt has been made to study the interaction of sodium morin-5-sulfonate (NaMSA) with the transport proteins, bovine serum albumin (BSA) employing UV-vis, fluorometric and circular dichroism (CD) techniques. The experimental results indicated that the quenching mechanism of BSA by the compound was a static procedure. Various binding parameters were evaluated. The negative value of ΔH, positive value of ΔS and the negative value of ΔG indicated that electrostatic interactions and hydrogen bonding play major roles in the binding of the NaMSA and BSA. Based on the Forster's theory of non-radiation energy transfer, the binding distance, r, between the donor (BSA) and acceptor (NaMSA) was evaluated. The results of CD and UV-vis spectroscopy showed that the binding of this complex to BSA induces some conformational changes in BSA.

In this study, an attempt has been made to study the interaction of sodium morin-5-sulfonate (NaMSA) with the transport proteins, bovine serum albumin (BSA) employing UV-vis, fluorometric and circular dichroism (CD) techniques.Figure optionsDownload as PowerPoint slideHighlights
► Morin (3,5,7,2′,4′-pentahydroxyflavone) is found in almonds, mill, fig and other moraceae which are used as dietary agents and also as herbal medicines.
► The interaction between BSA and flavonoids has attracted great interest among researchers for several decades
► Several spectroscopic techniques have been used in this research.