Binding constants and in silico analysis of albumin interaction with phenolic acids and flavonoids

Abstract

The interaction of bovine serum albumin with phenolic acids and flavonoids was studied by fluorescence spectroscopy under physiological conditions. Strong binding was observed in complexes with p-hydroxybenzoic acid and quercetin. Three-dimensional fluorescence spectra showed changes related to the backbone structures of the protein chain. Thermal denaturation studies and computational molecular docking indicated that caffeic acid and quercetin demonstrated optimal binding positions within the albumin structure, suggesting these compounds could significantly influence albumin transport function in vivo.