Filatova M P, Krit N A, Uskova N N, Maksimova E M, Gracheva I N, Reĭssmann Z
Bioorg Khim. 1991 May;17(5):690-6.
Inhibitors of the angiotensin-converting enzyme were synthesized by substituting N-and C-terminal amino acid residues of tripeptide Bz-Phe-Ala-Pro by the residues of 8-methoxy-5-sulphoquinoline and carboxy-1,2,3,4-tetrahydroquinoline, respectively, and their in vivo and in vitro biological activity was determined. The enzyme's S2' site proved to be non specific to the position of the carboxylic group in the C-terminal heterocyclic part of the inhibitor molecule. Introducing a modified quinoline residue into the N-terminal part of the inhibitor does not increase its specific interaction with the hydrophobic pocket of the angiotensin-converting enzyme.
通过分别用8-甲氧基-5-磺基喹啉残基和羧基-1,2,3,4-四氢喹啉残基取代三肽Bz-Phe-Ala-Pro的N端和C端氨基酸残基，合成了血管紧张素转换酶抑制剂，并测定了它们的体内和体外生物活性。结果证明，该酶的S2'位点对抑制剂分子C端杂环部分羧基的位置不具有特异性。在抑制剂的N端部分引入修饰的喹啉残基不会增加其与血管紧张素转换酶疏水口袋的特异性相互作用。
