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• W2593209281 abstract "The physicochemical properties of polybrominated diphenyl ethers are important for modeling their transport, but these data are often missing. Here, satisfactory bioactivity results were obtained using human serum albumin as the carrier, 2,2′,4,4′,5,6′-hexabromodiphenyl ether (BDE154) and 3-hydroxy-2,2′,4,4′, 5,6′-hexabromodiphenyl ether (3OH-BDE154) as the ligands, using UV–visible absorbance, fluorescence, circular dichroism, molecular docking, and molecular dynamics methods. The interactions between human serum albumin and BDE154 or 3OH-BDE154 were verified, consistent with the static quenching procedure. At pH 7.4, the binding constants of the complexes for site I were relatively comparable and increased in the order BDE154 < 3OH-BDE154. Then, the secondary structure and kinetic parameters of albumin were analyzed using the circular dichroism spectra and GROMACS software. The data obtained from these simulations indicate that hydrophobic attraction might be the key factor for the stability of complexes. The docking experiments provided further insight into the hydrophobic pocket and showed that 3OH-BDE154 has a stronger binding affinity to human serum albumin than BDE154. The experimental spectral data were obtained and compared with the simulation results, showing good agreement. A detailed analysis of PBDEs–HSA interactions would provide valuable information to better understand the interaction on this class of compounds." @default.
• W2593209281 created "2017-03-16" @default.
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• W2593209281 date "2017-04-01" @default.
• W2593209281 modified "2023-10-16" @default.
• W2593209281 title "Investigating the affinity of BDE154 and 3OH-BDE154 with HSA: Experimental and simulation validation" @default.
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• W2593209281 doi "https://doi.org/10.1016/j.etap.2017.03.004" @default.
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