Investigation on detoxication effects of 2-hydroxypropyl-β-cyclodextrin over two halogenated aromatic DBPs 2,4,6-trichlorophenol and 2,4,6-tribromophenol binding with human serum albumin

Abstract

The health effects of disinfection byproducts (DBPs) in drinking water drew great attention recently. Herein, by using in vitro (fluorescence quenching, UV absorbance, circular dichroism) and in silico (molecular docking) method, binding interactions of two halophenolic DBPs (2,4,6-trichlorophenol [TCP] and 2,4,6-tribromophenol [TBP]) with human serum albumin (HSA) and the influence of hydroxypropyl-beta-cyclodextrin (HPCD) on the interactions were investigated. TCP/TBP could form complexes with HSA mainly by hydrogen bonding, while changing its secondary structure, among which TBP showed more influential effect. Interestingly, the binding constants for halophenol-HSA complexes decreased obviously with the involvement of HPCD. Molecular docking results revealed that HPCD could include TCP/TBP into its cavity and change their original binding sites from subdomain IB to IIA, resulting in a more stable binding system. These findings are beneficial for understanding the toxicity of halophenols inside the human body and indicated that HPCD could be a promising detoxication agent for DBPs.

Keywords: Binding interaction; Detoxication; Disinfection byproducts; HSA; Halophenols.