Investigation of The Interaction Mechanism Between Lysozyme and Trichazol Using Fluorescence Spectroscopic Method

LIU Bao-sheng; HAN Rong; LI Zhi-yun; LI Tong-tong; LI Gai-xia

doi:10.3788/fgxb20153612.1458

您当前的位置：

首页 >

文章列表页 >

Investigation of The Interaction Mechanism Between Lysozyme and Trichazol Using Fluorescence Spectroscopic Method

更新时间：2020-08-12

- Investigation of The Interaction Mechanism Between Lysozyme and Trichazol Using Fluorescence Spectroscopic Method
- Chinese Journal of Luminescence Vol. 36, Issue 12, Pages: 1458-1463(2015)
- 作者机构：
  
  河北大学化学与环境科学学院河北省分析科学技术重点实验室,河北保定,071002
- 作者简介：
- 基金信息：
- DOI：10.3788/fgxb20153612.1458
  CLC： O657.3
- Received：21 June 2015，
  
  Revised：27 October 2015，
  
  Published：10 December 2015
- 稿件说明：
移动端阅览
刘保生, 韩荣, 李志云等. 硝基羟乙唑与溶菌酶反应机制的荧光光谱研究[J]. 发光学报, 2015,36(12): 1458-1463

LIU Bao-sheng, HAN Rong, LI Zhi-yun etc. Investigation of The Interaction Mechanism Between Lysozyme and Trichazol Using Fluorescence Spectroscopic Method[J]. Chinese Journal of Luminescence, 2015,36(12): 1458-1463
刘保生, 韩荣, 李志云等. 硝基羟乙唑与溶菌酶反应机制的荧光光谱研究[J]. 发光学报, 2015,36(12): 1458-1463 DOI： 10.3788/fgxb20153612.1458.

LIU Bao-sheng, HAN Rong, LI Zhi-yun etc. Investigation of The Interaction Mechanism Between Lysozyme and Trichazol Using Fluorescence Spectroscopic Method[J]. Chinese Journal of Luminescence, 2015,36(12): 1458-1463 DOI： 10.3788/fgxb20153612.1458.

摘要

分别在298

310

318 K温度下

利用荧光光谱法研究了pH=7.40生理条件下硝基羟乙唑(TRI)与溶菌酶(LYSO)的相互作用机理。结果表明

TRI与LYSO间通过静态猝灭方式相互作用。测定了LYSO与TRI反应的结合常数、结合位点数。利用反应过程的热力学参数

确定了LYSO-TRI体系的作用力类型;由Hill系数得出了LYSO或TRI的协同性;根据非辐射能量转移理论

确定了TRI到LYSO的结合距离

同时采用同步光谱法考察了TRI对LYSO构象的影响。

Abstract

The interaction mechanism of trichazol (TRI) to lysozyme(LYSO) at different temperatures (298

310

318 K) was investigated using fluorescence spectroscopy under simulative physiological conditions. The results clearly demonstrated that TRI caused strong quenching of the fluorescence of LYSO by a static quenching mechanism. The binding constants were order of magnitude of 10

and the number of binding site in the interaction was closed to 1. The thermodynamic parameters of LYSO-TRI system were determined as follows: negative

and positive

which indicated that electrostatic interaction played a major role in the binding reaction. The effect of cooperative binding of TRI was quantified by Hill's coefficient (

) and the values of

were slightly more than 1 in the systems

which indicated weakly positive cooperativeness in the interaction of TRI with LYSO. The binding distance (

) between TRI and LYSO was obtained based on the Frster nonradioactive resonance energy transfer and

was less than 7 nm. Furthermore

the effect of TRI on the conformation of LYSO was analyzed by using the synchronous fluorescence spectroscopy.

关键词

Keywords

references

Krishnamoorthy S, Shanmugam A, Malaichamy I. Probing the binding interaction of thionine with lysozyme: A spectroscopic and molecular docking investigation [J]. Dyes Pigments, 2015, 112:210-219.

Wang Z, Li D J, Jin J. Study on the interaction of puerarin with lysozyme by spectroscopic methods [J]. Spectrochim. Acta A, 2008, 70(4):866-870.

Li X Y. Interaction of metronidazole with bovine serum albumin by using fluorescence and resonance light scattering spectra [J]. Acta Phys. Chim. Sinica (物理化学学报), 2007, 23(2):262-267 (in Chinese).

Wang Q, He J W, Yan J, et al. Spectroscopy and docking simulations of the interaction between lochnericine and bovine serum albumin [J]. Luminescence, 2015, 30(2):240-246.

Teng Y, Ji F Y, Li C, et al. Interaction mechanism between 4-aminoantipyrine and the enzyme lysozyme [J]. J. Lumin., 2011, 131(12):2661-2667.

Wang W P, Min W N, Chen J R, et al. Binding study of diprophylline with lysozyme by spectroscopic methods [J]. J. Lumin., 2011, 131(4):820-824.

Paramaguru G, Kathiravan A, Selvaraj S, et al. Interaction of anthraquinone dyes with lysozyme: Evidences from spectroscopic and docking studies [J]. J. Hazard. Mater., 2010, 175(1-3):985-991.

Zhu J F, Li D G, Wu L M, et al. Binding analysis of farrerol to lysozyme by spectroscopic methods [J]. Spectrochim. Acta A, 2007, 68(2):354-359.

Ding F, Zhao G Y, Huang J L, et al. Fluorescence spectroscopic investigation of the interaction between chloramphenicol and lysozyme [J]. Eur. J. Med. Chem., 2009, 44(10):4083-4089.

Wang Y Q, Chen T T, Zhang H M. Investigation of the interactions of lysozyme and trypsin with biphenol A using spectroscopic methods [J]. Spectrochim. Acta A, 2010, 75(3):1130-1137.

Wang Y Q, Zhang H M, Zhang G C, et al. Interaction of the flavonoid hesperidin with bovine serum albumin: A fluorescence quenching study [J]. J. Lumin., 2007, 126(1):211-218.

Zhang G W, Chen X X, Guo J B, et al. Study on the interaction of hesperidin or icariin with lysozyme by fluorescence spectroscopy [J]. Spectrosc. Spect. Anal.(光谱学与光谱分析), 2009, 29(1):184-187 (in Chinese).

Xu Q, Deng D D, Cao Z J, et al. Interaction between serum albumin and four flavones by fluorescence spectroscopy and molecular docking [J]. Chin. J. Anal. Chem.(分析化学), 2010, 38(4):483-487 (in Chinese).

Liang H, Bian H D, Tu C Q, et al. Binding equilibrium study between La(Ⅲ) and HSA or BSA [J]. Chem. J. Chin. Univ.(高等学校化学学报), 2001, 22(1):21-25 (in Chinese).

Liu B S, Yang C, Wang J, et al. Luminescence mechanism study of the conjugation reaction between cefpirome sulfate and bovine serum albumin [J]. Chin. J. Lumin.(发光学报), 2011, 32(3):293-299 (in Chinese).

Zhao X C, Liu R T, Teng Y, et al. The interaction between Ag+ and bovine serum albumin: A spectroscopic investigation [J]. Sci. Total. Environ., 2011, 409(5):892-897.

Wang N, Ye L, Yan F F, et al. Spectroscopic studies on the interaction of azelnidipine with bovine serum albumin [J]. Int. J .Pharm., 2008, 351(1-2):55-60.

Li D J, Cao X X, Ji B M. Spectrophotometric studies on the interaction between myricetin and lysozyme in the absence or presence of Cu2+ or Fe3+ [J]. J. Lumin., 2010, 130(10):1893-1900.

Zhang G W, Chen X X, Guo J B, et al. Spectroscopic investigation of the interaction between chrysin and bovine serum albumin [J]. J. Mol. Struct., 2009, 921(1-3):346-351.

Hu Y Y, Xu S Q, Zhu X S, et al. Study on the interaction between methyl violet and bovine serum albumin by spectral analyses [J]. Spectrochim. Acta A, 2009, 74(2):526-531.

Views

112

下载量

CSCD

Alert me when the article has been cited

提交

Tools

Publicity Resources

Studies on The Interaction Mechanism Between Moxifloxacin and ctDNA by Fluorescence Spectroscopy

Modification on The Interaction Between Bovine Serum Albumin and Fluprofen by Improved Fluorescence Spectroscopy

The Effect of Metal Ions on Interaction Between Ethyl Piperate and Bovine Serum Albumin

Fluorescence Resonance Energy Transfer Between CdTe QDs and Rhodamine B with Its Application in The Determination of Lysozyme

Fluorescence Analysis of The Interaction Between Cefotaxime Sodium and Chloramphenicol as Well as Bovine Serum Albumin

Related Author

GUO Ying

ZHANG Li-hui

CAO Shi-na

CHONG Bao-hong

LING Xiao

BAO Li-er

WUYUN Suo-de

QU Ling-bo

Related Institution

河北大学化学与环境科学学院药物化学与分子诊断教育部重点实验室

河北大学化学与环境科学学院, 河北保定 071002

College of Chemistry and Chemical Engineering, Inner Mongolia University

The College of Chemistry and Molecular Engineering, Zhengzhou University

College of Chemistry and Chemical Engineering, Henan University of Tecnology, Zhengzhou 450001, China

AI问答

Address：No.3888 Dong Nanhu Road, Changchun, Jilin, China Postal code：130033
Tel：0431-86176862 Email：fgxbt@126.com
Technical support is provided by Beijing Founder electronics co., LTD 吉ICP备11002662号-17 京公网安备11010802024621
It is recommended to read the content of this site in Chrome&IE9+. Please switch to extreme mode in browser 360.
Cookies We use cookies to help provide and enhance our service and tailor content. By continuing, you agree to the use of cookies.

⁰