n-Dodecyl β-D-maltoside specifically competes with general anesthetics for anesthetic binding sites.
n-Dodecyl β-D-maltoside specifically competes with general anesthetics for anesthetic binding sites.
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n-十二烷基β-D-麦芽糖苷专门与全身麻醉剂竞争麻醉剂结合位点。
DOI：
10.1080/07391102.2013.838699
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发表时间：
2014
影响因子：
4.4
通讯作者：
Liu,Renyu
中科院分区：
文献类型：
--
作者：
Xu,Longhe;Matsunaga,Felipe;Xi,Jin;Li,Min;Ma,Jingyuan;Liu,Renyu
我们最近证明，阴离子洗涤剂十二烷基硫酸钠（SDS）特异性地与马脾脱铁蛋白，一种可溶性蛋白质，其在受体中模拟麻醉剂结合位点的麻醉剂结合位点相互作用。这增加了其他去污剂与麻醉剂类似地相互作用并封闭这些位点的可能性，从而阻止了新麻醉剂结合位点的正确鉴定。正十二烷基β-D-麦芽糖苷（DDM）是一种非离子去污剂，由于其温和和非变性性质，常用于蛋白质麻醉剂研究。在这项研究中，我们证明，SDS和DDM占据麻醉剂的模型蛋白质人血清白蛋白（HSA）和马脾脱铁蛋白的结合位点，从而抑制全身麻醉剂丙泊酚和异氟烷的结合。DDM与HSA（Kd= 40 μM）的特异性相互作用亲和力低于SDS（Kd= 2 μM）。DDM发挥所有这些作用，同时不干扰任何模型蛋白的天然结构。计算结果证实了实验结果，证明DDM和两种麻醉剂的模型蛋白的结合位点重叠。总的来说，我们的研究结果表明，DDM和SDS特异性地与麻醉剂结合位点相互作用，从而可能阻止新的麻醉剂位点的识别。当使用SDS和DDM等去污剂进行蛋白质麻醉研究并解释结果时，应采取特殊预防措施。
We recently demonstrated that the anionic detergent sodium dodecyl sulfate (SDS) specifically interacts with the anesthetic binding site in horse spleen apoferritin, a soluble protein which models anesthetic binding sites in receptors. This raises the possibility of other detergents similarly interacting with and occluding such sites from anesthetics, thereby preventing the proper identification of novel anesthetic binding sites.n-Dodecyl β-D-maltoside (DDM) is a non-ionic detergent commonly used during protein-anesthetic studies because of its mild and non-denaturing properties. In this study, we demonstrate that SDS and DDM occupy anesthetic binding sites in the model proteins human serum albumin (HSA) and horse spleen apoferritin and thereby inhibit the binding of the general anesthetics propofol and isoflurane. DDM specifically interacts with HSA (Kd= 40 μM) with a lower affinity than SDS (Kd= 2 μM). DDM exerts all these effects while not perturbing the native structures of either model protein. Computational calculations corroborated the experimental results by demonstrating that the binding sites for DDM and both anesthetics on the model proteins overlapped. Collectively, our results indicate that DDM and SDS specifically interact with anesthetic binding sites and may thus prevent the identification of novel anesthetic sites. Special precaution should be taken when undertaking and interpreting results from protein-anesthetic investigations utilizing detergents like SDS and DDM.