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本文根据Metcalf等定性讨论N-甲基氨甲酸取代苯酯抑制家蝇胆碱酯酶的构效关系,并参考骨架式分子模型,观察到抑制剂的亲电性双正键和酶表面带负电性的酯解部位之间,只有抑制剂苯环一侧的邻、间位(即2,3位)基团有可能与酶表面的阴离子部位相互结合,且其契合程度与邻位基团的长度及间位基团的宽度有关。据此,作者用抑制剂苯环上邻、间位取代基的立体参数及双正键的键正性,对活性强度作回归分析来探讨其规律性。
According to Metcalf et al., Qualitatively discussed the structure-activity relationship of N-methylcarbamate-substituted phenyl ester in house flies cholinesterase, and with reference to the scaffold molecular model, it was observed that the electrophilic double positive bond of the inhibitor and the surface of the enzyme negatively charged Sexual esterification sites, only the inhibitor benzene ring side of the ortho, meta (2,3) groups may be the enzyme surface and the anionic sites of mutual binding, and its degree of compatibility with the ortho group Length and the width of meta groups. Based on this, the author uses the three-dimensional parameters of the ortho and meta substituents on the benzene ring of the inhibitor and the bond positive of the bidentate bond to investigate the regularity of the activity intensity by regression analysis.