Department of Chemistry, University of Prishtina, Str. "Nëna Terezë" p.n. 10 000 Prishtina,Kosova.
Faculty of Medicine, University of Prishtina, Str. Bulevardi i Dëshmorëve, p.n. 10 000 Prishtina,Kosova.
Curr Protein Pept Sci. 2021;22(10):729-744. doi: 10.2174/1389203722666210916141924.
Angiotensin-converting enzyme (ACE) shares some homologies with ACE2. However, they are not inhibited by the same inhibitors, but both are associated primarily with the hypertensive disorder through the renin-angiotensin system (RAS). The principal activity of ACE2 is to metabolize Ang II into the vasodilatory Ang-(1-7). The ongoing COVID-19 pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has brought the ACE2 to the center of attention. This coronavirus uses the host cell ACE2 protein to enter and infect the epithelial cells. In light of the virus's entrance into human cells, the differences in the molecular basis of ACE2 among affected patients may cause their different responses to the virus. Many details about the specific interaction between the viral S protein and ACE2 are already reported. To date, some effective clinically approved vaccines are in use globally, and many others are under development, but no effective specific therapeutic drugs are available against COVID-19. Inhibitors, especially peptide inhibitors, have a great potential to be used for the treatment of COVID-19 and other possible emerging diseases caused by viral pathogens. As a result of the well-known viral protein structures and their host cell targets such as ACE2, antiviral peptides could be appropriately designed and optimized for therapeutic purposes. A better understanding of the structure and pathophysiology of the ACE2 receptor and the interplay between the viral S protein and ACE2 may help to find the solution for the virus treatment. This review summarizes the current understanding of S protein interaction with the ACE2 protein as a potential specific target against SARS-CoV-2 and strategies using peptides against COVID-19.
血管紧张素转换酶（ACE）与 ACE2 具有某些同源性。然而，它们不受相同抑制剂的抑制，但两者都主要通过肾素-血管紧张素系统（RAS）与高血压疾病相关。ACE2 的主要活性是将 Ang II 代谢为血管扩张的 Ang-（1-7）。由严重急性呼吸系统综合症冠状病毒 2（SARS-CoV-2）引起的持续的 COVID-19 大流行使 ACE2 成为关注的焦点。这种冠状病毒利用宿主细胞 ACE2 蛋白进入并感染上皮细胞。鉴于该病毒进入人体细胞，受影响患者中 ACE2 的分子基础的差异可能导致他们对病毒的不同反应。关于病毒 S 蛋白与 ACE2 之间具体相互作用的许多细节已经有报道。迄今为止，一些有效的临床批准疫苗在全球范围内使用，许多其他疫苗正在开发中，但针对 COVID-19 没有有效的特效治疗药物。抑制剂，特别是肽抑制剂，具有很大的潜力用于治疗 COVID-19 和其他可能由病毒病原体引起的新兴疾病。由于众所周知的病毒蛋白结构及其宿主细胞靶标，如 ACE2，可以为治疗目的适当设计和优化抗病毒肽。更好地了解 ACE2 受体的结构和病理生理学以及病毒 S 蛋白与 ACE2 之间的相互作用，可能有助于找到治疗病毒的方法。本综述总结了目前对 S 蛋白与 ACE2 蛋白相互作用的理解，ACE2 蛋白作为针对 SARS-CoV-2 的潜在特异性靶标，以及针对 COVID-19 使用肽的策略。
