An odorant-binding protein facilitates odorant transfer from air to hydrophilic surroundings in the blowfly.
An odorant-binding protein facilitates odorant transfer from air to hydrophilic surroundings in the blowfly.
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DOI：
10.1093/chemse/bji049
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发表时间：
2005-09
期刊：
影响因子：
3.5
通讯作者：
K. Tsuchihara;K. Fujikawa;M. Ishiguro;Takuji Yamada;C. Tada;K. Ozaki;M. Ozaki
中科院分区：
文献类型：
--
作者：
K. Tsuchihara;K. Fujikawa;M. Ishiguro;Takuji Yamada;C. Tada;K. Ozaki;M. Ozaki
化学感觉相关亲脂性配体结合蛋白（CRLBP）是一种昆虫气味结合蛋白（OBP），广泛存在于丽蝇的味觉和嗅觉器官中。通过计算构建，一个CRLBP的三维分子模型显示良好的拟合荧光配体，7-羟基香豆素（7-HC），在其配体结合口袋。通过显示与CRLBP结合的7-HC的荧光在天然电泳凝胶中迁移，我们证实CRLBP与7-HC形成稳定的复合物。在气味剂结合实验中，7-HC蒸汽气味通过曝气引入到含有CRLBP的水溶液中，并通过荧光光谱定量其与CRLBP的结合。由于嗅觉器官以及味觉器官的苍蝇响应蒸汽，我们建议，CRLBP有效地转移气味从空气中到水生环境中形成稳定的复合物与空气中的分子在两个化学感觉器官。
Chemical sense-related lipophilic ligand-binding protein (CRLBP) is an insect odorant-binding protein (OBP) found abundantly in the taste and olfactory organs of the blowfly, Phormia regina. Through computational construction, a three-dimensional molecular model of a CRLBP indicated good fitting to a fluorescent ligand, 7-hydroxycoumarin (7-HC), in its ligand-binding pocket. By showing that the fluorescence of 7-HC bound to CRLBP migrated in a native electrophoresis gel, we confirmed that CRLBP formed a stable complex with 7-HC. In an odorant-binding experiment, 7-HC vapor odor was introduced by aeration to the aquatic solution containing CRLBP and its binding to CRLBP fluorospectrometrically quantified. Because olfactory organs as well as taste organs of flies respond to vapors, we suggest that CRLBP effectively transfers odorants from the air into aquatic surroundings by forming stable complexes with airborne molecules in both chemosensory organs.