title: Interaction of diuron to human serum albumin: Insights from spectroscopic and molecular docking studies.
abstract: This investigation was undertaken to determine the interaction of diuron with human serum albumin (HSA) was studied by monitoring the spectral behavior of diuron-HSA system. The fluorescence of HSA at 340 nm excited at 230 nm was obviously quenched by diuron due to dynamic collision and the quenching constant was of the order of 10(4) L mol(-1) at 310 K. However, no fluorescence quenching was observed when excited at 280 nm. Thermodynamic investigations revealed that the combination between diuron and HSA was entropy driven by predominantly hydrophobic interactions. The binding of diuron induced the drastic reduction in α-helix conformation and the significant enhancement in β-turn conformation of HSA. In addition, both sites marker competition study and molecular modeling simulation evidenced the binding of diuron to HSA primarily took place in subdomain IIIA (Sudlow's site II).
authors.affiliation: a School of Civil & Environmental Engineering, and National International Cooperation Base on Environment and Energy, University of Science and Technology Beijing , Beijing , P.R. China.
authors.forename: Huilun
authors.initials: H
authors.lastname: Chen
authors.affiliation: a School of Civil & Environmental Engineering, and National International Cooperation Base on Environment and Energy, University of Science and Technology Beijing , Beijing , P.R. China.
authors.forename: Honghao
authors.initials: H
authors.lastname: Rao
authors.affiliation: a School of Civil & Environmental Engineering, and National International Cooperation Base on Environment and Energy, University of Science and Technology Beijing , Beijing , P.R. China.
authors.forename: Jian
authors.initials: J
authors.lastname: Yang
authors.affiliation: a School of Civil & Environmental Engineering, and National International Cooperation Base on Environment and Energy, University of Science and Technology Beijing , Beijing , P.R. China.
authors.forename: Yongxiang
authors.initials: Y
authors.lastname: Qiao
authors.affiliation: a School of Civil & Environmental Engineering, and National International Cooperation Base on Environment and Energy, University of Science and Technology Beijing , Beijing , P.R. China.
authors.forename: Fei
authors.initials: F
authors.lastname: Wang
authors.affiliation: a School of Civil & Environmental Engineering, and National International Cooperation Base on Environment and Energy, University of Science and Technology Beijing , Beijing , P.R. China.
authors.forename: Jun
authors.initials: J
authors.lastname: Yao
mesh_terms: D001665:Binding Sites; D004237:Diuron / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics; D014364:Tryptophan / Q000737:chemistry
chemical_list: D012709:Serum Albumin; D014364:Tryptophan; D004237:Diuron
keywords: Diuron; human serum albumin; molecular docking; spectroscopy; toxicity