Angiotensin-Converting Enzyme 2 Activation Is Not a Common Feature of Angiotensin-Converting Enzyme Inhibitory Peptides

Zihan Wang, Hongbing Fan, Xiaoyu Bao, Jianping Wu

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Angiotensin-converting enzyme (ACE) catalyzes the formation of angiotensin II (Ang II), a vasoconstrictor, whereas its homologue ACE2 degrades Ang II into angiotensin (1-7) (Ang (1-7)), a vasodilator. Given the similarities in structure and their interconnected roles in the regulation of cardiovascular system, this study aims to investigate if ACE-inhibitory (ACEi) peptides can also activate ACE2. About 200 potent ACEi peptides were subjected to molecular docking, 20 peptides were selected for cell and in vitro enzymatic activity studies, and 5 peptides were fed orally to spontaneously hypertensive rats at a dose of 15 mg/kg body weight/day for 7 days. Peptides IKW and RIY showed significant antihypertensive activity with activated circulating/aortic ACE2, circulating Ang (1-7), and decreased Ang II levels. IQY reduced blood pressure, increased Ang (1-7) level, but did not affect ACE and ACE2. Peptides MAW and MRW did not affect blood pressure, ACE, and ACE2. Our study showed that ACE2 activation is not a common feature of ACEi peptides.

Original languageEnglish
Pages (from-to)8867-8876
Number of pages10
JournalJournal of Agricultural and Food Chemistry
Volume71
Issue number23
DOIs
StatePublished - Jun 14 2023

Bibliographical note

Publisher Copyright:
© 2023 American Chemical Society

Keywords

  • A7r5 cells
  • ACE inhibitors
  • ACE2 activators
  • bioactive peptides
  • molecular docking
  • spontaneously hypertensive rats

ASJC Scopus subject areas

  • General Chemistry
  • General Agricultural and Biological Sciences

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