Abstract
Despite the phenolic acids' health benefits, their interactions with proteins are still unclear. In this study, the interactions of Bovine Serum Albumin (BSA) with chlorogenic acid (CHA), caffeic acid (CA), and their Al3+, Cu2+ complexes were studied by using circular dichroism (CD) spectroscopy, fluorescence spectroscopy, and UV/Vis spectroscopy. It was found that esterification of carboxyl group of CA with quinic acid increased the binding affinities for BSA. After chelating with Cu2+ and Al3+, both CHA and CA exhibited high binding affinities for BSA. CHA could form CHA-Cu2 and CHA-Al2 complex with Cu2+ and Al3+. The result of CD spectroscopy demonstrated that the binding of CHA and Al3+ with BSA contributed to the folding of BSA secondary structure. In addition, with the presence of CHA, binding with Al3+ could also induce changes in BSA conformation. The binding sites of both CHA and CA were closed to Trp213.
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