论文部分内容阅读
目的对αB-芋螺毒素VxXXIVA与其受体α9α10乙酰胆碱受体(nAChR)之间的结合特性进行研究。方法利用非洲爪蟾卵母细胞表达大鼠α9α10乙酰胆碱受体,通过变换膜电压,以及与α-芋螺毒素RgIAm的竞争性结合实验,测定α9α10乙酰胆碱受体电流与洗脱速率的变化。结果αB-芋螺毒素VxXXIVA与具有竞争性结合特性的α-芋螺毒素的结合位点有部分重叠,但又不完全相同,是1个新的微位点,其受体结合活性随膜电压的升高而不会改变,不具有电压依赖性。结论获知了具有独特结构的αB-VxXXIVA与受体α9α10nAChR之间的结合特性,该研究结果将为αB-VxXXIVA作为工具药开发、α9α10nAChR受体结构与功能的研究、以及基于该受体为药靶的药物设计提供理论基础。
OBJECTIVE: To investigate the binding properties of αB-conotoxin VxXXIVA to its receptor α9α10 acetylcholine receptor (nAChR). Methods The rat α9α10 acetylcholine receptor was expressed by Xenopus laevis oocytes and the changes of α9α10 acetylcholine receptor currents and elution rates were determined by changing the membrane voltage and the competitive binding assay with α-conotoxin RgIAm. Results αB-conotoxin VxXXIVA and competitive conjugation of α-conotoxine binding sites have some overlap, but not exactly the same, is a new micro-site, its receptor binding activity with the membrane voltage The increase will not change, not voltage-dependent. CONCLUSIONS The binding properties between αB-VxXXIVA and receptor α9α10 nAChR with unique structure were obtained. The results of this study will be the development of αB-VxXXIVA as a tool drug and the study of the structure and function of α9α10 nAChR receptor. Based on this receptor as a drug target The drug design provides the theoretical basis.