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Toxic Interaction between Dibutyl Phthalate and Human Serum Albumin: Spectroscopic and Molecular Modeling Investigations
Author(s) -
Yuan Dong,
Shen Zhonglan,
Liu Rutao,
Wei Peihai,
Gao Canzhu
Publication year - 2014
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.201300206
Subject(s) - chemistry , dibutyl phthalate , human serum albumin , circular dichroism , in vivo , hydrophobic effect , molecular model , fluorescence , amino acid residue , phthalate , plasma protein binding , biophysics , transporter , binding site , biochemistry , stereochemistry , organic chemistry , peptide sequence , gene , physics , microbiology and biotechnology , quantum mechanics , biology
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 ΔH and ΔS. 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.