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Yue C.,Anhui University of Technology | Yue C.,Peking University | Fang D.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Liu L.,Huaihai Institute of Technology | Yi T.-F.,Anhui University of Technology
Journal of Molecular Liquids | Year: 2011

This paper took various types of the task-specific ionic liquids as the main to review their synthesis and application to organic unit reactions from the point of view of development and practical utility. The economical task-specific ionic liquids were also brought forward. © 2011 Elsevier B.V. All Rights Reserved. Source


Wang Y.-Q.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Zhang H.-M.,Yancheng Teachers University
Journal of Photochemistry and Photobiology B: Biology | Year: 2015

Abstract Bisphenol A and its analogues have carcinogenic potentials and toxicities. However, there are lacks of studies elucidating gene toxic interactions of bisphenols with DNA. In this work, the binding modes of five bisphenol compounds with calf thymus DNA were characterized. The multi-spectroscopic experimental results indicated that the fluorescence quenching of bisphenols by calf thymus DNA point to groove binding. The ultraviolet visible and circular dichroism spectral data displayed that bisphenols partly induced conformational changes of calf thymus DNA. In addition, the binding constants of bisphenol A, diphenolic acid, bisphenol AF, bisphenol AP, bisphenol fluorine with calf thymus DNA obtained from fluorescence emission spectra were 1.09 × 104, 3.65 × 104, 4.46 × 104, 1.69 × 104, 4.49 × 104 L mol-1 at 298.15 K, which indicated that the multi-noncovalent binding forces were involved in the binding processes. In silico investigations indicated that DNA has the preferable binding sites binding with bisphenols by minor groove binding and electrons transfer from DNA bases to bisphenols occurred. In addition, the structural differences of these five bisphenols partly affected the binding ability of them with DNA. © 2015 Elsevier B.V. Source


Wang Y.-Q.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Wang Y.-Q.,Yancheng Teachers University | Zhang G.-C.,Yancheng Teachers University | Zhang H.-M.,Yancheng Teachers University
Journal of Solution Chemistry | Year: 2011

The interactions between pentachlorophenol (PCP) and jack bean urease were studied using UV/vis absorption, CD, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectroscopic techniques. The fluorescence data showed that the fluorescence quenching of urease by PCP the results of the formation of a PCP-urease complex involving a hydrophobic interaction. The distance r between the donor (urease) and acceptor (PCP) was obtained from the fluorescence resonance energy transfer. The effect of PCP on the conformation of urease was analyzed using UV/vis absorption, synchronous fluorescence and three-dimensional fluorescence spectroscopic techniques. The result showed that PCP can enter into the hydrophobic pocket at the interface of urease and that the micro environments around the tyrosine and tryptophan residues were changed. © 2011 Springer Science+Business Media, LLC. Source


Wang Y.-Q.,Yancheng Teachers University | Zhang H.-M.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Cao J.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Tang B.-P.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection
Journal of Photochemistry and Photobiology B: Biology | Year: 2014

Interactions of bisphenol S, a new bisphenol analogue with bovine serum albumin and calf thymus DNA were investigated using different spectroscopic methods and molecular modeling calculation. According to the analysis of experimental and theoretical data, we concluded that hydrophobic interactions and hydrogen bonding primarily mediated the binding processes of bisphenol S with bovine serum albumin and DNA. In addition, the electrostatic force should not be excluded. Molecular modeling studies indicated that the binding site of bisphenol S to bovine serum albumin located in the subdomain IB, while bisphenol S was a groove binder of DNA. In addition, BPS did not obviously induce second structural changes of bovine serum albumin, but it induced a conformational change of calf thymus DNA. © 2014 Elsevier B.V. All rights reserved. Source


Wang Y.-Q.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Wang Y.-Q.,Yancheng Teachers University | Zhang H.-M.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Zhang H.-M.,Yancheng Teachers University
Journal of Agricultural and Food Chemistry | Year: 2013

To explore the binding mechanism of phthalate plasticizers with digestive proteases, their effects on conformation and activity of pepsin by multispectroscopic approach and molecular modeling were investigated. Fluorescence spectra combined with UV-vis and circular dichroism (CD) spectra measurements indicated that the six phthalate plasticizers induced the changes of tertiary and secondary structure of pepsin. The solvent polarity of environment around both Trp and Tyr residues on pepsin were affected by phthalate plasticizers. By analyzing the fluorescence quenching and theoretical calculation data, it was concluded that a binding site exists for each phthalate plasticizer in pepsin with different binding ability. The hydrophobic, hydrogen bonding, and π-π stacking interactions were involved in the interactions between pepsin and phthalate plasticizers. Moreover, the activity assay indicated that phthalate plasticizers were not powerfully inhibitors or activators for pepsin. These studies demonstrated that phthalate plasticizers could cause some negative effects on pepsin. The present studies may provide a way to analyze the biological safety of phthalate plasticizers on digestive proteases or other proteins. © 2013 American Chemical Society. Source

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