Structure-affinity relationship of the binding of phenolic acids and their derivatives to bovine serum albumin

Abstract

Phenolic acids perform biological effects which are largely influenced by their binding to serum albumin. Therefore, investigating structure-affinity relationship of binding between phenolic acids and serum albumin is important. In this study, 114 phenolic acids and their derivatives, sharing the benzoic acid core with different substituents groups, were selected to investigate structure-affinity relationships with bovine serum albumin. The binding constants were obtained through fluorescence quenching, and a comprehensive mathematical model with inner-filter effect correction was applied. The results showed that the hydroxy group at the 2-position led to stronger binding affinity, while it had a negative influence at the 4-position. Substituting hydroxy groups with methoxy groups at 4-position and with methyl groups at 3-position both strengthened the binding affinity, respectively. Hydrogen bonding was one of the key binding forces for this binding interaction. Our findings provide a fundamental insight on the binding mechanism of phenolic acids to bovine serum albumin.

Keywords: Binding affinity; Bovine serum albumin; Fluorescence quenching; Gallic acid (PubChem CID: 370); Gentisic acid (PubChem CID: 3469); Isovanillic acid (PubChem CID: 12575); Phenolic acids; Protocatechuic acid (PubChem CID: 72); Salicylic acid (PubChem CID: 338); Syringic acid (PubChem CID: 10742); Vanillic acid (PubChem CID: 8468).