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根据假设的血管紧张素转换酶(ACE)活性部位的模型,酶与底物或抑制剂之间相互作用,其C-端的酰胺键是重要因素之一,酰胺羰基的氧和酶中的质子供体之间形成氢键。又根据酰胺键的电子和几何特征,以及考虑到C-N键之间的平面性和部份双键化的特性,因此合成了一系列化合物(表Ⅰ,Ⅱ),并进行了抑制ACE的活性试验。化合物24和25活性的明显差异,表明前者对ACE的结合酰胺键起了重要作用。非环的第二酰胺(24)和N一甲基取代的第三酰胺(26)具有相似的活性,因此否定了第二酰
According to the hypothetical model of the active site of angiotensin converting enzyme (ACE), the interaction of an enzyme with a substrate or inhibitor whose amide bond at the C-terminus is an important factor, the oxygen of the amide carbonyl and the proton donation in the enzyme The formation of hydrogen bonds between the body. A series of compounds (Tables I, II) were synthesized based on the electronic and geometric characteristics of the amide bond and taking into account the planarity and partial double bonding between the CN bonds and the ACE inhibitory activity assay . Significant differences in the activity of compounds 24 and 25 indicate that the former plays an important role in ACE binding to amide bonds. The acyclic second amide (24) and N-methyl-substituted third amide (26) have similar activities, thus negating the second acyl