Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection

Yancheng, China

Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection

Yancheng, China

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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.


Wang Y.-Q.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Wang Y.-Q.,Yancheng Teachers University | Chen T.-T.,Nantong University | Zhang H.-M.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Zhang H.-M.,Yancheng Teachers University
Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy | Year: 2010

The interaction between bisphenol A (BPA) and lysozyme (or trypsin) was investigated by UV-vis absorption, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. BPA effectively quenched the intrinsic fluorescence of lysozyme and trypsin via static quenching. H-bonds and van der Waals interactions played a major role in stabilizing the BPA-proteinase complex. The distance r between donor and acceptor was obtained to be 1.65 and 2.26 nm for BPA-lysozyme and BPA-trypsin complexes, respectively. The effect of BPA on the conformation of lysozyme and trypsin was analyzed using synchronous fluorescence and three-dimensional fluorescence spectra. © 2010 Elsevier B.V. All rights reserved.


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.


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
Journal of Photochemistry and Photobiology B: Biology | Year: 2014

Herein, we studied the binding interactions between hydroxylated single-walled carbon nanotubes and hemoglobin and myoglobin by the use of multi-spectral techniques and molecular modeling. The ultraviolet-vis absorbance and circular dichroism spectral results indicated that the binding interactions existed between hydroxylated single-walled carbon nanotubes and hemoglobin/myoglobin. These binding interactions partially affected the soret/heme bands of hemoglobin and myoglobin. The secondary structures of hemoproteins were partially destroyed by hydroxylated single-walled carbon nanotubes. Fluorescence studies suggested that the complexes formed between hydroxylated single-walled carbon nanotubes and hemoglobin/myoglobin by hydrogen bonding, hydrophobic, and π-π stacking interactions. In addition, molecular modeling analysis well supported the experimental results. © 2014 Elsevier B.V. All rights reserved.


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.


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 | Tang B.-P.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection
Journal of Photochemistry and Photobiology B: Biology | Year: 2010

The nature of the interaction between human hemoglobin and C.I. acid red 27 was investigated systematically by ultraviolet-vis absorbance, circular dichroism, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques at pH 7.40. The quenching mechanism, binding constants, and the number of binding sites were determined by the quenching of human hemoglobin fluorescence in presence of C.I. acid red 27. The results showed that the nature of the quenching was of static type and the process of binding acid red 27 on human hemoglobin was a spontaneous molecular interaction procedure. The electrostatic and hydrophobic interactions played a major role in stabilizing the complex; The distance r between donor and acceptor was obtained to be 4.40. nm according to Förster's theory; The effect of acid red 27 on the conformation of human hemoglobin was analyzed using synchronous fluorescence, circular dichroism and three-dimensional fluorescence spectra. © 2010 Elsevier B.V.


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.


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.


Zhang G.-C.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Zhang G.-C.,Yancheng Teachers University | Xu J.-Y.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Xu J.-Y.,Yancheng Teachers University | And 2 more authors.
Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy | Year: 2012

The interaction between Cr 2O 7 2- and human serum albumin (HSA) was investigated using fluorescence, UV/vis, FT-IR, CD spectroscopy, and molecular modeling method. The experimental results showed that the fluorescence quenching of HSA by Cr 2O 7 2- is a result of the formation of HSA-chromium(VI) complex; static quenching was confirmed to result in the fluorescence quenching. The corresponding thermodynamic parameters showed that the process of binding Cr 2O 7 2- on HSA was a spontaneous molecular interaction procedure. Ionic, H-bonds and van der Waals interactions play a major role in stabilizing the complex. The Cr 2O 7 2- altered the environments of Trp and Tyr residues in HSA. © 2011 Elsevier B.V. All rights reserved.


Zhang H.-M.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Zhang H.-M.,Yancheng Teachers University | Cao J.,Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection | Cao J.,Yancheng Teachers University | And 4 more authors.
Chemico-Biological Interactions | Year: 2014

TiO2 nanoparticles are the most widely used metal oxide nanoparticles and have oxidative toxicity. Catalase is an important antioxidant enzyme. Here the understanding of an effect of TiO2 nanoparticles on the activity and structure of catalase is crucial to characterize the toxicity of TiO2 nanoparticles. These experimental data revealed that TiO 2 nanoparticles could bind to catalase by the electrostatic and hydrogen bonding forces. On binding TiO2 nanoparticles, catalase got destabilized with the decrease of α-helices content, the solvent polarity of environment around the fluorescence chromophores on catalase were also affected. In addition, TiO2 nanoparticles also affected the activity of catalase. TiO2 nanoparticles acted as an activator of catalase activity at a low molar concentration and as an inhibitor at a higher molar concentration. With regard to human health, the present study could provide a better understanding of the potential nanotoxicity of TiO2 nanoparticles. © 2014 Elsevier Ireland Ltd. All rights reserved.

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