Two novel angiotensin I-converting enzyme inhibitory peptides from garlic protein: In silico screening, stability, antihypertensive effects in vivo and underlying mechanisms

Abstract

This study aimed to screen novel angiotensin I-converting enzyme (ACE) inhibitory peptides from garlic proteins and to explore their underlying antihypertensive mechanisms in vivo. After simulated hydrolysis and in silico screening, two novel peptides (MGR and HDCF) were obtained with the highest ACE inhibitory activity (IC50 of 4.50 μM and 26.38 μM) and acted as competitive inhibitors. They interacted with key residues in the ACE receptor mainly through hydrogen bonding and exhibited excellent stability against high temperature, extreme pH, and gastrointestinal digestion. In spontaneously hypertensive rats, MGR and HDCF effectively lowered blood pressure after single or continuous treatments. This was mainly achieved by balancing the renin-angiotensin system, improving renal and cardiac impairment, and regulating endothelial dysfunction. These findings suggested that garlic proteins were potentially suitable materials to prepare ACE inhibitory peptides and provided two promising candidates for ACE inhibition as functional food ingredients.