Weller H N, Gordon E M, Rom M B, Pluscec J
Biochem Biophys Res Commun. 1984 Nov 30;125(1):82-9. doi: 10.1016/s0006-291x(84)80337-x.
Modification of alanyl proline by introduction of both zinc coordinating and S1 subsite binding interactions affords potent new carboxy- and mercapto-acyl dipeptide angiotensin-converting enzyme (ACE) inhibitors. Design of these inhibitors was guided by an extension of the hypothetical ACE active site model originally used to derive captopril. Significant increases in ACE inhibitory activity were observed by introduction of conformation constraint into acyclic acyl dipeptides, thus further defining the three dimensional structure of the ACE active site.
通过引入锌配位和S1亚位点结合相互作用来修饰丙氨酰脯氨酸，可得到有效的新型羧基和巯基酰基二肽血管紧张素转换酶（ACE）抑制剂。这些抑制剂的设计以最初用于推导卡托普利的假设ACE活性位点模型的扩展为指导。通过在无环酰基二肽中引入构象限制，观察到ACE抑制活性显著增加，从而进一步确定了ACE活性位点的三维结构。
