Characterization of binding interaction of triclosan and bovine serum albumin

Abstract

Triclosan (TCS) is widely used in personal care products and acts as an antibacterial agent. Residues of TCS may have potential effects on the human health. In this article, the interaction between TCS and bovine serum albumin (BSA) has been characterized by using multi-spectroscopic approaches and molecular docking method under physiological conditions. Thermodynamic investigations revealed that TCS spontaneously bound to a binding site of BSA and hydrogen bonds played a dominant role in this process. The site marker competition experiments indicated that TCS bound at site II (subdomain IIIA) of BSA, which was well substantiated by molecular docking. The binding of TCS further led to changes of conformation and microenvironment of BSA. This work explored the interaction of TCS with BSA, which might be beneficial for evaluating the binding mechanism of other environmental pollutant at molecular level.