Investigation of the Interaction between Isoflavonoids and Bovine Serum Albumin by Fluorescence Spectroscopy

✍ Scribed by Ling-Bo Qu; Xiao-Lan Chen; Ran Yang; Ling Wang; Hua-Jin Zeng

• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 77 KB
• Volume: 25
• Category: Article
• ISSN: 0256-7660
• DOI: 10.1002/cjoc.200790215

✦ Synopsis

Abstract

The interactions of bovine serum albumin (BSA) with three structurally related isoflavonoids, genistein, puerarin and daidzein, were studied under physiological conditions by fluorescence spectroscopic technique. The quenching mechanism of these compounds with BSA was suggested as static quenching and the binding constants were determined at different temperatures based on the fluorescence quenching results. The transfer efficiency of energy and distance between the acceptor and BSA were investigated on the basis of the mechanism of the Förster energy transference. According to the thermodynamic parameters it has been suggested that the acting force be mainly hydrophobic force. The comparison of binding potency of the three isoflavonoids to BSA showed that the substitution by 5‐OH and 8‐Glc could enhance the binding affinity. All these obtained in the work can make us better understand the mode of the action and pharmacological activities of the isoflavonoids.