高等学校化学学报

高等学校化学学报 ›› 2011, Vol. 32 ›› Issue (6): 1284.

• 研究论文 • 上一篇    下一篇

荧光光谱法研究中华蜜蜂化学感受蛋白与特异配基的相互作用

李红亮, 张林雅, 朱丽云, 倪翠侠, 商晗武   

  1. 中国计量学院生命科学学院, 生物计量及检验检疫技术浙江省重点实验室, 杭州 310018
  • 收稿日期:2010-07-19 修回日期:2010-10-25 出版日期:2011-06-10 发布日期:2011-05-10
  • 通讯作者: 商晗武 E-mail:hwshang@cjlu.edu.cn
  • 基金资助:

    国家自然科学基金(批准号: 30900163, 30571241)、 浙江省重大农业科技专项(批准号: 2006C12020)和浙江省自然科学基金(批准号: Y307597)资助.

Interaction of Chemosensory Proteins of Apis cerana cerana with Special Ligands by Fluorescence Spectroscopy

LI Hong-Liang, ZHANG Lin-Ya, ZHU Li-Yun, NI Cui-Xia, SHANG Han-Wu*   

  1. College of Life Sciences, Key Laboratory of Biometrology and Inspection & Quarantine of Zhejiang Province, China Jiliang University, Hangzhou 310018, China
  • Received:2010-07-19 Revised:2010-10-25 Online:2011-06-10 Published:2011-05-10
  • Contact: SHANG Han-Wu E-mail:hwshang@cjlu.edu.cn
  • Supported by:

    国家自然科学基金(批准号: 30900163, 30571241)、 浙江省重大农业科技专项(批准号: 2006C12020)和浙江省自然科学基金(批准号: Y307597)资助.

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被引次数

4

摘要： 用荧光光谱法研究了中华蜜蜂化学感受蛋白(chemosensory proteins, CSPs)3与其特异性配基N-苯基-1-萘胺(N-Phenyl-1-naphthylamine, 1-NPN)的相互作用关系。研究表明1-NPN能使CSP3在328 nm (λem)处产生猝灭，且猝灭机理为静态猝灭，另外猝灭过程中ΔH0 > 0, ΔS0 > 0，表明二者间的主要作用力为疏水相互作用。依据F?rster非辐射能量转移机制，得到二者的结合距离为9.3 nm，能量转移效率E = 0.054。根据同步荧光技术考察1-NPN对CSP3的构象的影响，表明CSP3荧光主要贡献者——色氨酸残基的最大发射波长略有红移，表明原处于疏水腔中的色氨酸残基由于所处环境的极性增加，而使CSP3构象产生变化。

关键词: 中华蜜蜂, 化学感受蛋白, 相互作用, 荧光光谱

Abstract: The interactions of separated and purified recombinant Chemosensory proteins 3 (CSP3) of Chinese honeybee, Apis cerana cerana with its special ligands, N-Phenyl-1-naphthylamine (1-NPN) was investigated with the method of fluorescence spectroscopy. The results showed that 1-NPN could quench the intrinsic fluorescence of CSP3 at 328 nm (λem) by static quenching and hydrophobic interaction was the predominant intermolecular force, and the binding distance (r = 9.3 nm) and energy-transfer efficiency (E = 0.054) bewteen donor (CSP3) and acceptor (1-NPN) were obtained according to the F?rster-type dipole-dipole nonradiative energy-transfer mechanism. In addition, from the results of synchronous fluorescence spectroscopy, the tryptophan residue contributed the main fluorescent emission, and with its λmax turnning to red shift, it indicated that 1-NPN can affect the the conformation of CSP3, and increase the polarity of tryptophan residue in the hydrophobic cavity of CSP3.

Key words: Apis cerana cerana, chemosensory protein, interaction, fluorescence spectroscopy

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