Multi-spectroscopic and computational evaluation on the binding of sinapic acid and its Cu(II) complex with bovine serum albumin. (15th December 2019)

• Record Type: Journal Article
• Authors: Sengupta, Priti; Pal, Uttam; Mondal, Prasenjit; Bose, Adity
• Is Part Of: Food chemistry. Volume 301(2019)
• Publication Date: 2019-12-15
• Subjects: Sinapic acid -- Metal complex -- BSA -- Fluorescence quenching -- Molecular docking; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2019.125254
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Binding interaction of sinapic acid and its Cu 2+ complex with BSA was investigated. A static quenching mechanism was involved in the interaction process in both cases. Binding and thermodynamic parameters were evaluated for both the systems. In both systems, site I (subdomain IIA) was the preferred binding site. Biological assay was performed to compare the anti-oxidant activities of two compounds. Abstract: Researches based on metal complexes of plant-derived phenolic acids have attracted much attention due to their beneficial applications in the development of functional food products, dietary supplements and pharmacology. Binding of phenolic acids with serum proteins greatly influences their pharmacological properties. In this context, interactions of a naturally occurring phenolic acid, sinapic acid (SA) and its Cu 2+ complex with a model transport protein, bovine serum albumin (BSA), have been explored by means of different spectroscopic and theoretical tools. Spectroscopic studies revealed that the interaction of SA and its Cu 2+ complex with BSA occurred through quenching of intrinsic fluorescence of BSA. Site-specific experimental and docking studies were performed to predict the binding site. The geometies of bound Cu 2+ and interacting residues of protein were predicted from a solution dynamics study. Interestingly, the complexation of SA with Cu 2+ enhanced the antioxidant activity of SA.