Minimum structural requirement for an inhalational anesthetic binding site on a protein target.
Minimum structural requirement for an inhalational anesthetic binding site on a protein target.
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蛋白质靶标上吸入麻醉剂结合位点的最低结构要求。
DOI：
10.1016/0304-4165(95)00187-5
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Eckenhoff,RG
中科院分区：
文献类型：
--
作者：
Johansson,JS;Eckenhoff,RG
本研究利用直接光亲和标记、荧光光谱和圆二色光谱研究了吸入麻醉剂氟烷与不带电的α-螺旋形式的聚（L-赖氨酸）在一定链长范围内的相互作用。氟烷与长链均聚物（190至1060个残基）特异性结合，在大于300个残基的聚合物中达到1氟烷对160个赖氨酸残基的稳定化学计量。氟烷仅与α-螺旋30残基聚合物和所有带电无规卷曲形式的聚合物非特异性结合。这些数据表明，氟烷结合是超二级结构的功能，从而在较长的聚合物中形成分子内螺旋-螺旋簇，从而产生受限的疏水结构域。圆二色谱法不能证明在任何链长的聚（L-赖氨酸）的二级结构的变化与高达12 mM的氟烷，这表明广泛的氢键破坏麻醉剂不会发生。
The present study makes use of direct photoaffinity labeling and fluorescence and circular dichroism spectroscopy to examine the interaction of the inhalational anesthetic halothane with the uncharged α-helical form of poly(l-lysine) over a range of chain lengths. Halothane bound specifically to long chain homopolymers (190 to 1060 residues), reaching a stable stoichiometry of 1 halothane to 160 lysine residues in polymers longer than 300 residues. Halothane bound only non-specifically to an α-helical 30 residue polymer and to all of the polymers in their charged, random coil form. The data suggest that halothane binding is a function of supersecondary structure whereby intramolecular helix-helix clusters form in the longer polymers, resulting in the creation of confined hydrophobic domains. Circular dichroism spectroscopy cannot demonstrate changes in poly(l-lysine) secondary structure at any chain length with up to 12 mM halothane, suggesting that extensive hydrogen bond disruption by the anesthetic does not occur.