Ward J M, Cockcroft V B, Lunt G G, Smillie F S, Wonnacott S
Department of Biochemistry, University of Bath, UK.
FEBS Lett. 1990 Sep 17;270(1-2):45-8. doi: 10.1016/0014-5793(90)81231-c.
The ability of methyllycaconitine (MLA) to inhibit the binding of [125I]alpha-bungarotoxin to rat brain membranes, frog and human muscle extracts and the human muscle cell line TE671 has been measured. MLA showed a markedly higher affinity for the rat brain site (Ki 1.4 x 10(-9) M) than for the muscle receptors (Ki 10(-5)-10(-6) M). Structure modelling techniques were used to fit the structure of MLA to a nicotinic pharmacophore model. MLA is the first low molecular weight ligand to be shown to discriminate between muscle nicotinic receptors and their alpha-bungarotoxin-binding counterpart in the brain, and as such may be a useful structural probe for pursuing the structural and functional properties of the neuronal protein.
已测定甲基lycaconitine（MLA）抑制[125I]α-银环蛇毒素与大鼠脑膜、青蛙和人类肌肉提取物以及人类肌肉细胞系TE671结合的能力。MLA对大鼠脑部位（Ki 1.4×10^(-9) M）的亲和力明显高于对肌肉受体的亲和力（Ki 10^(-5)-10^(-6) M）。采用结构建模技术将MLA的结构与烟碱药效团模型进行拟合。MLA是首个被证明能区分肌肉烟碱受体及其在脑中的α-银环蛇毒素结合对应物的低分子量配体，因此可能是研究神经元蛋白结构和功能特性的有用结构探针。
