Transport of angiotensin converting enzyme and renin dual inhibitory peptides LY, RALP and TF across Caco-2 cell monolayers. (August 2017)

• Record Type: Journal Article
• Authors: Yang, Yi-Jie; He, Hai-Yan; Wang, Feng-Zhang; Ju, Xing-Rong; Yuan, Jian; Wang, Li-Feng; Aluko, Rotimi E.; He, Rong
• Is Part Of: Journal of functional foods. Volume 35(2017)
• Page Start: 303
• Page End: 314
• Publication Date: 2017-08
• Subjects: Angiotensin converting enzyme -- Renin -- Bioactive peptides -- Caco-2 cell -- Peptide transport -- Rapeseed; Functional foods -- Analysis -- Periodicals; Food -- Biotechnology -- Periodicals; Nutrition -- Periodicals; 613.2
• DOI: 10.1016/j.jff.2017.05.053
• Languages: English
• ISSNs: 1756-4646

Abstract

Highlights: The stability of the ACE- and renin-inhibitory peptides was investigated. The inhibition activity was estimated by non-linear regression analysis. LY had the potential to be transported intact into blood circulation. The fragments of RALP after transport had potential ACE- and renin- activity. Abstract: In order for peptides to exert physiological effects, intact transportation or absorption of their degradation fragments with bioactive potency is required. In this study, Caco-2 cell model was employed to investigate the stability of ACE- and renin-inhibitory peptides LY, RALP and TF during cellular absorption. Apparent permeability coefficient was 3.49, 0.32, and 0.94 × 10 −6 cm/s for LY, RALP and TF, respectively. LY had the highest infiltration yield of 6.59%, compared to RALP (0.51%) and TF (2.44%) at 180 min. Peptides collected from the basolateral sides after 180 min had ACE-inhibitory levels of 33.03%, 14.22% and 14.33% with different initial concentrations for LY (2 mM), RALP (1 mM) and TF (3 mM), respectively. In contrast, renin-inhibitory activities were lower at 9.52% (LY) and 7.37% (RALP) while TF had no inhibition. Thus, dipeptides could be more easily absorbed for controlling hypertension and the fragments of RALP had potential antihypertensive properties.