Angiotensin I–converting enzyme–inhibitory peptides from bovine collagen: insights into inhibitory mechanism and transepithelial transport

• Published in: Food research international Vol. 89; no. Pt 1; pp. 373 - 381
• Main Authors: Fu, Yu, Young, Jette Feveile, Rasmussen, Martin Krøyer, Dalsgaard, Trine Kastrup, Lametsch, René, Aluko, Rotimi E., Therkildsen, Margrethe
• Format: Journal Article
• Language: English
• Published: Canada Elsevier Ltd 01.11.2016
• Subjects: angiotensin I-converting enzyme; Collagen peptides; digestive enzymes; molecular docking; non-competitive inhibition; transepithelial transport; Collagen peptides; transepithelial transport; angiotensin I-converting enzyme; non-competitive inhibition; molecular docking; digestive enzymes
• ISSN: 0963-9969; 1873-7145
• DOI: 10.1016/j.foodres.2016.08.037

The inhibitory mechanism and transepithelial transport of angiotensin I-converting enzyme (ACE)-inhibitory peptides (VGPV and GPRGF) derived from Alcalase®- and papain-hydrolyzed bovine collagen were investigated. The inhibitory mechanism of VGPV and GPRGF was experimentally determined to be non-competitive and the results were supported by molecular docking data. In silico and in vitro gastrointestinal digestion indicated that VGPV remained resistant to digestive enzymes, while GPRGF was degraded into smaller ACE-inhibitory peptides (GPR and GF). VGPV and GPRGF were transported across monolayers of human intestinal epithelial Caco-2 cells through paracellular pathway and retained their ACE-inhibitory activities. The present study suggests that VGPV and GPRGF may possibly be absorbed and exert antihypertensive effects in vivo. [Display omitted] •A novel collagen-derived ACE-inhibitory peptide was identified.•VGPV and GPRGF remained stable towards digestive enzymes.•Collagen-derived ACE-inhibitory peptides were non-competitive inhibitors.•VGPV and GPRGF were transported across Caco-2 cell monolayers via the paracellular pathway.