US EPA

2510967 

Journal Article 

Toxic interaction between dibutyl phthalate and human serum albumin: Spectroscopic and molecular modeling investigations 

Yuan, D; Shen, Z-L; Liu, R-T; Wei, P-H; Gao, C-Z 

2014 

Yes 

Journal of the Chinese Chemical Society
ISSN: 0009-4536 

61 

2 

255-262 

10.1002/jccs.201300206 

WOS:000337634200008 

Because of the widely usage of Dibutyl phthalate (DBP), its residue exist extensively in the environment and can enter human body, being potential harmful. Human serum albumin (HSA) is a major transporter for endogenous and exogenous compounds in vivo. The aim of this study was to examine the interaction of HSA with DBP through spectroscopic and molecular modeling methods. The experiments revealed that DBP binds to site I (subdomain IIA) of HSA mainly through hydrophobic interactions, illustrated by the calculated Delta H and Delta S. Furthermore, molecular docking was applied to define the specific binding sites, the results of which show that DBP mainly interacts with the positively charged amino acid residues LEU 219, PHE 223, LEU 234, LEU 238, ALA 258, LEU 260, and ILE 290 predominately through hydrophobic interactions, in accordance with the conclusion of thermodynamic analysis. The binding of DBP can cause conformational and some microenvironmental changes of HSA, revealed by UV-vis absorption, synchronous fluorescence, and circular dichroism results. The accurate and full basic data in the work is beneficial to clarifying the binding mechanism of DBP with HSA in vivo and understanding its effect on protein function during the blood transportation process. 

Dibutyl phthalate; Human serum albumin; Fluorescence spectra; UV-vis absorption spectra; Molecular modeling