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通过表面等离子体共振分析检测BmK IT2与哺乳动物和昆虫钠通道的结合情况。

The binding of BmK IT2 on mammal and insect sodium channels by surface plasmon resonance assay.

作者信息

Chai Zhi-Fang, Bai Zhan-Tao, Liu Tong, Pang Xue-Yan, Ji Yong-Hua

机构信息

Graduate School of the Chinese Academy of Sciences, Shanghai Institute of Physiology, Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, PR China.

出版信息

Pharmacol Res. 2006 Aug;54(2):85-90. doi: 10.1016/j.phrs.2006.02.009. Epub 2006 Mar 8.

DOI:10.1016/j.phrs.2006.02.009
PMID:16616856
Abstract

The binding of BmK IT2 to insect and mammal sodium channels was investigated by surface plasmon resonance technique. The results showed that BmK IT2 could bind not only to cockroach neuronal membranes but also to rat cerebrocortical and hippocampal synaptosomes with distinct affinity. The binding of BmK IT2 could be competed significantly by BmK AS and BmK abT, but not by AaH II, BmK I and veratridine. Furthermore, BmK alphaIV could partially inhibit the binding of BmK IT2 to rat cerebrocortical synaptosomes and cockroach neuronal membranes, but not to rat hippocampal synaptosomes. These results suggested that BmK IT2 had diverse binding properties on the mammal and insect sodium channels.

摘要

利用表面等离子体共振技术研究了BmK IT2与昆虫和哺乳动物钠通道的结合情况。结果表明,BmK IT2不仅能与蟑螂神经元膜结合,还能以不同亲和力与大鼠大脑皮质和海马突触体结合。BmK IT2的结合能被BmK AS和BmK abT显著竞争,但不能被AaH II、BmK I和藜芦碱竞争。此外,BmK alphaIV可部分抑制BmK IT2与大鼠大脑皮质突触体和蟑螂神经元膜的结合,但不能抑制其与大鼠海马突触体的结合。这些结果表明,BmK IT2在哺乳动物和昆虫钠通道上具有多种结合特性。

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Exploring the obscure profiles of pharmacological binding sites on voltage-gated sodium channels by BmK neurotoxins.探索蜂毒素对电压门控钠离子通道的药理学结合位点的未知特征。
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Localization of receptor site on insect sodium channel for depressant β-toxin BmK IT2.
昆虫钠离子通道上抑制剂 β-毒素 BmK IT2 的受体位点定位。
PLoS One. 2011 Jan 14;6(1):e14510. doi: 10.1371/journal.pone.0014510.
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