Investigation on The Interaction of Nifedipine and Pepsin Fluorescent Groups by Synchronous Fluorescence Spectroscopy

MA Li-hua; LIU Bao-sheng; BIAN Gang; WANG Chun-dan; ZHANG Hong-cai; CHENG Xu

doi:10.3788/fgxb20183912.1792

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Investigation on The Interaction of Nifedipine and Pepsin Fluorescent Groups by Synchronous Fluorescence Spectroscopy

更新时间：2020-08-12

- Investigation on The Interaction of Nifedipine and Pepsin Fluorescent Groups by Synchronous Fluorescence Spectroscopy
- Chinese Journal of Luminescence Vol. 39, Issue 12, Pages: 1792-1798(2018)
- 作者机构：
  
  河北大学化学与环境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：
  
  Supported by National Natural Science Foundation of China(21375032)
- DOI：10.3788/fgxb20183912.1792
  CLC： O657.3
- Received：22 March 2018，
  
  Revised：05 July 2018，
  
  Published Online：26 July 2018，
  
  Published：05 December 2018
- 稿件说明：
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马丽花, 刘保生, 边刚等. 同步荧光法探究硝苯地平与胃蛋白酶荧光基团的作用机制[J]. 发光学报, 2018,39(12): 1792-1798

MA Li-hua, LIU Bao-sheng, BIAN Gang etc. Investigation on The Interaction of Nifedipine and Pepsin Fluorescent Groups by Synchronous Fluorescence Spectroscopy[J]. Chinese Journal of Luminescence, 2018,39(12): 1792-1798
马丽花, 刘保生, 边刚等. 同步荧光法探究硝苯地平与胃蛋白酶荧光基团的作用机制[J]. 发光学报, 2018,39(12): 1792-1798 DOI： 10.3788/fgxb20183912.1792.

MA Li-hua, LIU Bao-sheng, BIAN Gang etc. Investigation on The Interaction of Nifedipine and Pepsin Fluorescent Groups by Synchronous Fluorescence Spectroscopy[J]. Chinese Journal of Luminescence, 2018,39(12): 1792-1798 DOI： 10.3788/fgxb20183912.1792.

摘要

以同步荧光法研究了298，310，318 K下硝苯地平（NDP）与胃蛋白酶（PEP）的荧光基团酪氨酸残基（P-Tyr）、色氨酸残基（P-Trp）之间的相互作用。表明药物以动态猝灭的方式猝灭P-Tyr、P-Trp的荧光，结合位点数

为1，主要作用力是疏水作用。310 K时NDP与PEP氨基酸残基反应的荧光猝灭比率份数P-Trp 53.43%

P-Tyr 46.57%，结合位置更靠近P-Trp，NDP与蛋白结合率P-Tyr:69.43%~87.15%，P-Trp:73.64%~90.60%，分别建立了结合模型。且Hill系数

约为1，该结合与后继配体无协同作用。结合距离

都小于7 nm，则NDP与P-Tyr、P-Trp之间都存在非辐射能量转移。

Abstract

The interactions between fluorophore tyrosine residues(P-Tyr) and tryptophan residues (P-Tyr) of pepsin(PEP) and nifedipine(NDP) at 298

310 and 318 K were studied by synchronous fluorescence spectroscopy. The results showed that the drug quenches the fluorescence of P-Tyr and P-Trp by means of dynamic quenching. The number of binding sites was 1

and the main force was hydrophobicity. The fluorescence quenching ratio of NDP to PEP amino acid residues at 310 K was P-Trp 53.43%

P-Tyr 46.57%

meaning the binding site was closer to P-Trp. The binding rates of NDP to protein were P-Tyr:69.43%-87.15% and P-Trp:73.64%-90.60%

established a binding model

respectively. The Hill coefficient

was about 1

meaning this combination has no synergistic effect with subsequent ligand. The binding distance

was less than 7 nm in both cases. Thus

non-radiative energy transfer exists between NDP and P-Tyr as well as between NDP and P-Trp.

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Keywords

references

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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, 国家级化学实验教学示范中心(河北大学)

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School of Pharmaceutical Sciences, Zhengzhou University

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