Evaluation the binding of chlorogenic acid with bovine serum albumin: Spectroscopic methods, electrochemical and molecular docking.

Chlorogenic acid(CGA) is the common active phenolic acid in Chinese medicinal materials such as honeysuckle and eucommia. It is a class of small molecules with multiple activities such as antioxidant, inhibiting cancer cells, lowering blood sugar and lowering blood pressure. In this paper, UV-vis spectroscopy, fluorescence spectroscopy, circular dichroism, molecular dynamics simulation and cyclic voltammetry (CV) electrochemical analysis were used to investigate the mechanism about interaction between CGA and BSA. Based on fluorescence quenching analysis, CGA quenched the inherent fluorescence of BSA remarkably through a static mechanism. The obtained value of binding constant (K = 5.75 × 10 L·mol) revealed a high binding affinity between CGA and BSA. The simulated molecular docking showed that hydrophobic force were also involved in the interaction between BSA and CGA. This paper also investigate the effect of temperature and metal ions on the binding of CGA and BSA. When the temperature increased, the binding of BSA and CGA was destroyed. Metal ions affect both the structure of BSA and the combination of BSA and CGA. By studying the mechanism of CGA interaction with BSA, we elucidated the storage and transport mechanism of CGA in vivo under simulated human environment and temperature conditions.