ACE抑制肽构效关系及其酶法制备的研究进展

高血压是一种全球性的公共健康问题。血管紧张素转换酶(angiotensin converting enzyme,ACE)作为一种二肽缩肽酶,通过肾素-血管紧张素系统和激肽释放酶-激肽系统(kallikrein-kinin system,KKS)对血压进行调节。近年来,已有许多从各种食源蛋白中获得ACE抑制肽的研究报道。相比于化学合成药物,食源性蛋白获得的ACE抑制肽在治疗高血压方面更具安全性和温和性。许多研究已经探讨了食源性降压肽的构效关系,尤其是多肽一级序列对活性的影响。目前,最常用于制备ACE抑制肽的方式是酶催化水解蛋白,包括使用单酶或复合酶对蛋白进行水解。本文将主要对ACE抑制肽构效关系和酶法制备ACE抑制肽的研究进展进行综述,以期为获得优良的ACE抑制肽产品提供理论指导。

Progress in Structure-Activity Relationship and Enzymatic Preparation of ACE Inhibitory Peptides

Hypertension is a considerable public health problem worldwide. Angiotensin-Ⅰ converting enzyme (dipeptidylcarboxypeptidase, EC 3.4.15.1, ACE) plays a critical role in regulating blood pressure through the renninangiotensin system (RAS) and kallikrein-kinnin system (KKS). Recently, numerous studies aimed at alleviating hypertension have focused on the generation and isolation of ACE-inhibitory peptides from various food sources. A number of studies have reported the structure-activity relationship of food protein-derived antihypertensive peptides, especially the effect of the primary structure on the potency. Compared with synthetic chemical drugs, ACE inhibitory peptides derived from food proteins are considered to be safer and milder. Nowadays, one of the most widely used techniques to liberate ACE inhibitory peptides is enzymatic hydrolysis. This technique involves one or more proteases at the optimum temperature and pH conditions. In this review, in order to provide a theoretical guidance for the preparation of high-quality ACE inhibitory peptides, we review recent reports on the structure-activity relationship and enzymatic preparation of ACE inhibitory peptides.