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  • Title: Study on the interaction of sodium morin-5-sulfonate with bovine serum albumin by spectroscopic techniques.
    Author: Shahabadi N, Mohammadpour M.
    Journal: Spectrochim Acta A Mol Biomol Spectrosc; 2012 Feb; 86():191-5. PubMed ID: 22057301.
    Abstract:
    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.
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