Effects of normal alcohols and isoflurane on lipid headgroup dynamics in nicotinic acetylcholine receptor-rich lipid vesicles.
Effects of normal alcohols and isoflurane on lipid headgroup dynamics in nicotinic acetylcholine receptor-rich lipid vesicles.
复制标题
正常醇和异氟烷对富含烟碱乙酰胆碱受体的脂质囊泡中脂质头基动力学的影响。
DOI：
10.1016/s0005-2736(00)00285-6
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Firestone,LL
中科院分区：
文献类型：
--
作者：
Seto,T;Firestone,LL
证据的趋势表明，全身麻醉药直接作用于神经膜中的蛋白质。然而，烟碱型乙酰胆碱受体的功能（钠渗透性、脱敏率）受其在其中重构的膜的组成调节的事实被认为是乙酰胆碱受体与膜之间相互作用的变化的结果。在这项研究中，蛋白质-脂质相互作用的水平上的脂质头基的研究，使用电子顺磁共振（EPR）和头基自旋标记。脂质头基流动性进行了评价与旋转相关时间从EPR谱。在头基深度的蛋白质-脂质相互作用被证明从光谱的运动限制组件。由于蛋白质-脂质相互作用，旋转相关时间从7 ns增加到13 ns。研究了麻醉剂（乙醇、1-己醇和异氟醚）对蛋白质-脂质相互作用的影响，相关时间为13 ns。它的结论是，在这项研究中使用的麻醉剂没有改变蛋白质-脂质相互作用的水平上的脂质头基，到目前为止所观察到的旋转相关时间，不排除麻醉剂，扰乱蛋白质-脂质相互作用通过这种机制调节受体功能的可能性。
The trend of evidence suggests that general anesthetics act directly on proteins in the neural membrane. However, the fact that the functions of nicotinic acetylcholine receptor (sodium permeability, desensitization rate) are modulated by the composition of the membrane in which it is reconstituted has been thought to be a result of the variation of interactions between acetylcholine receptor and membrane. In this study, protein–lipid interaction at the level of the lipid headgroup was investigated using electron paramagnetic resonance (EPR) and headgroup spin label. Lipid headgroup mobility was evaluated with rotational correlation time from the EPR spectrum. Protein–lipid interaction at headgroup depth was demonstrated from the motionally restricted component of the spectrum. Rotational correlation time increased to 13 ns from 7 ns due to protein–lipid interaction. The effect of anesthetic (ethanol, 1-hexanol, and isoflurane) on protein–lipid interaction was investigated, and the correlation time was 13 ns. It is concluded that the anesthetics used in this study did not alter protein–lipid interaction at the level of the lipid headgroup, so far as observed by rotational correlation time, without excluding the possibility that anesthetics that perturb protein–lipid interactions modulate receptor functions via this mechanism.