Department of Pharmacy, University of Patras, Panepistimioupoli-Rion, GR-26504, Greece.
J Pept Sci. 2010 Feb;16(2):91-7. doi: 10.1002/psc.1201.
Human ACE is a central component of the renin-angiotensin system and a major therapeutic target for cardiovascular diseases. The somatic form of the enzyme (sACE) comprises two homologous metallopeptidase domains (N and C), each bearing a zinc active site with similar but distinct substrate and inhibitor specificities. In this study, we present the biological activity of silacaptopril, a silylated analogue of captopril, and its binding affinity towards ACE. Based on the recently determined crystal structures of both the ACE domains, a series of docking calculations were carried out in order to study the structural characteristics and the binding properties of silacaptopril and its analogues with ACE.
人血管紧张素转换酶是肾素-血管紧张素系统的核心组成部分，也是心血管疾病的主要治疗靶点。该酶的体细胞形式（sACE）由两个同源金属肽酶结构域（N 和 C）组成，每个结构域都有一个锌活性位点，具有相似但不同的底物和抑制剂特异性。在这项研究中，我们介绍了 silacaptopril 的生物学活性，silacaptopril 是 captopril 的硅烷化类似物，以及它与 ACE 的结合亲和力。基于最近确定的 ACE 结构域的晶体结构，进行了一系列对接计算，以研究 silacaptopril 及其类似物与 ACE 的结构特征和结合特性。
