Aprison M H, Lipkowitz K B, Simon J R
J Neurosci Res. 1987;17(3):209-13. doi: 10.1002/jnr.490170302.
Strychnine, a complex molecule, antagonizes in some unknown manner the action of glycine, an important inhibitory neurotransmitter in the spinal cord and brainstem of many vertebrates. To help understand the mechanism of this antagonism, we have employed modern computational methods to assess the similarities between these seemingly different molecules. An exhaustive comparison of topological and electronic features of both molecules was made. We have successfully located a glycine-like fragment in the strychnine molecule that, when compared to glycine, exhibits both topological and electronic charge congruence. The successful location of this glycine-like fragment allows us to speculate how the large strychnine molecule assumes its role as an antagonist against the inhibitory action of glycine, the simplest amino acid.
士的宁是一种复杂分子，它以某种未知方式拮抗甘氨酸的作用，甘氨酸是许多脊椎动物脊髓和脑干中一种重要的抑制性神经递质。为了帮助理解这种拮抗作用的机制，我们采用了现代计算方法来评估这些看似不同的分子之间的相似性。对这两种分子的拓扑和电子特征进行了详尽比较。我们成功地在士的宁分子中定位到了一个类似甘氨酸的片段，与甘氨酸相比，它在拓扑和电荷方面都表现出一致性。这个类似甘氨酸片段的成功定位使我们能够推测出大的士的宁分子是如何发挥其作为针对最简单氨基酸——甘氨酸抑制作用的拮抗剂的作用的。
