Molecular interactions, bioavailability, and cellular mechanisms of angiotensin‐converting enzyme inhibitory peptides. Issue 1 (22nd August 2018)

• Record Type: Journal Article
• Authors: Fan, Hongbing; Liao, Wang; Wu, Jianping
• Is Part Of: Journal of food biochemistry. Volume 43:Issue 1(2019)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2018-08-22
• Subjects: ACE inhibitory peptides -- angiotensin converting enzyme (ACE) -- bioavailability -- cellular mechanisms -- molecular docking -- vascular endothelial cells -- vascular small muscle cells; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; Biochemistry -- Periodicals; 664.024
• DOI: 10.1111/jfbc.12572
• Languages: English
• ISSNs: 0145-8884

Abstract

Abstract: Food‐derived angiotensin‐converting enzyme inhibitory (ACEi) peptides have gained substantial interest as potential alternatives to synthetic drugs in the management of hypertension. Peptide size and sequence are two critical factors that determine their potency, bioavailability, and cellular mechanisms. Molecular interaction studies between ACE and ACEi peptides support that potent ACEi peptides are generally composed of hydrophobic, positively charged, and aromatic or cyclic amino acid residues at the third, second, and first position from the C‐terminus, respectively. Small peptides containing N‐terminal Tyr and/or C‐terminal Pro could improve their stability against enterocyte peptidases, thus their bioavailability. Different ACEi peptides can reduce aberrant cellular proliferation, excessive inflammation, and oxidative stress but through different mechanisms. Further understanding the structure–activity–bioavailability relationships will help design novel potent ACEi peptides with improved bioavailability and in vivo efficacy. Practical applications: ACEi peptides have the potential for uses as functional food ingredients against hypertension.