ACE抑制肽构效关系研究进展

血管紧张素转化酶(angiotensin-converting enzyme,ACE)抑制肽是一类从食源性蛋白质中分离得到的具有降高血压活性的多肽。由于其降血压效果好,而且没有降压药物的毒副作用从而引起了广泛关注。近年来,ACE抑制肽的构效关系研究成为研究重点。结构生物信息学研究表明,ACE抑制肽的ACE抑制能力不仅与其分子质量有关,而且与其氨基酸序列以及其立体空间构象之间存在高度相关性。ACE抑制肽的抑制类型与ACE抑制活性、构效关系也存在一定相关性。对ACE抑制肽构效关系进行深入研究将有助于指导开发高活性的功能性食品及降血压药物。

Progress in Research on Structure-Activity Relationship of ACE Inhibitory Peptides

Angiotensin converting enzyme (ACE) inhibitory peptides are a category of peptides derived from food proteins which can reduce blood pressure. ACE inhibitory peptides have gained extensive concerns because they can reduce blood pressure without side effects as antihypertensive drugs. In recent years, the structure-activity relationship of ACE inhibitory peptides has become one of the research focuses. Structural bioinformatics showed that the activity of ACE inhibitory peptides is related to not only their molecular masses, but also their amino acid sequences and spatial conformation. It is also found that the type of inhibit of ACE inhibitory peptides is related to their activity and structure-activity relationship. Intensive studies on ACE inhibitory peptide structure-activity relationship will be helpful to guide the development of new functional foods and antihypertensive drugs.