Tags

Type your tag names separated by a space and hit enter

Transepithelial transport and stability in blood serum of angiotensin-I-converting enzyme inhibitory dipeptides.
Z Naturforsch C J Biosci. 2008 May-Jun; 63(5-6):451-9.ZN

Abstract

The dipeptides Ala-Trp, Val-Phe, and Val-Tyr inhibit the angiotensin-I-converting enzyme. They are encrypted within the primary sequences of different food proteins, e.g. milk proteins. The angiotensin-I-converting enzyme inhibitory potency of these synthetic dipeptides was quantified using a spectrophotometric assay. The dipeptides showed no adverse effects on differentiated Caco-2 cells (model for human intestinal epithelium), as confirmed by transepithelial electrical resistance, microscopy and the activity of the brush-border enzyme dipeptidyl aminopeptidase IV. Furthermore, the transport of these bioactive dipeptides through intact Caco-2 monolayers and their stability to incubation in human blood serum has been demonstrated for the first time. Low molecular mass peptides represent the minimal structures required for angiotensin-I-converting enzyme inhibition which have a high potential bioavailability. Therefore, they may act as target peptides in enriched hydrolysates for the preparation of an angiotensin-I-converting enzyme inhibitory peptide and for the use in special formulations as functional foods/foods of specified health use.

Authors+Show Affiliations

Max-Rubner-Institute (MRI), Federal Research Institute of Nutrition and Food-Location Kiel, Department of Safety and Quality of Milk and Fish Products, Hermann-Weigmann-Str. 1, D-24103 Kiel, Germany.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18669035

Citation

Pentzien, Anne-Kathrin, and Hans Meisel. "Transepithelial Transport and Stability in Blood Serum of angiotensin-I-converting Enzyme Inhibitory Dipeptides." Zeitschrift Fur Naturforschung. C, Journal of Biosciences, vol. 63, no. 5-6, 2008, pp. 451-9.
Pentzien AK, Meisel H. Transepithelial transport and stability in blood serum of angiotensin-I-converting enzyme inhibitory dipeptides. Z Naturforsch, C, J Biosci. 2008;63(5-6):451-9.
Pentzien, A. K., & Meisel, H. (2008). Transepithelial transport and stability in blood serum of angiotensin-I-converting enzyme inhibitory dipeptides. Zeitschrift Fur Naturforschung. C, Journal of Biosciences, 63(5-6), 451-9.
Pentzien AK, Meisel H. Transepithelial Transport and Stability in Blood Serum of angiotensin-I-converting Enzyme Inhibitory Dipeptides. Z Naturforsch, C, J Biosci. 2008 May-Jun;63(5-6):451-9. PubMed PMID: 18669035.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Transepithelial transport and stability in blood serum of angiotensin-I-converting enzyme inhibitory dipeptides. AU - Pentzien,Anne-Kathrin, AU - Meisel,Hans, PY - 2008/8/2/pubmed PY - 2008/8/30/medline PY - 2008/8/2/entrez SP - 451 EP - 9 JF - Zeitschrift fur Naturforschung. C, Journal of biosciences JO - Z. Naturforsch., C, J. Biosci. VL - 63 IS - 5-6 N2 - The dipeptides Ala-Trp, Val-Phe, and Val-Tyr inhibit the angiotensin-I-converting enzyme. They are encrypted within the primary sequences of different food proteins, e.g. milk proteins. The angiotensin-I-converting enzyme inhibitory potency of these synthetic dipeptides was quantified using a spectrophotometric assay. The dipeptides showed no adverse effects on differentiated Caco-2 cells (model for human intestinal epithelium), as confirmed by transepithelial electrical resistance, microscopy and the activity of the brush-border enzyme dipeptidyl aminopeptidase IV. Furthermore, the transport of these bioactive dipeptides through intact Caco-2 monolayers and their stability to incubation in human blood serum has been demonstrated for the first time. Low molecular mass peptides represent the minimal structures required for angiotensin-I-converting enzyme inhibition which have a high potential bioavailability. Therefore, they may act as target peptides in enriched hydrolysates for the preparation of an angiotensin-I-converting enzyme inhibitory peptide and for the use in special formulations as functional foods/foods of specified health use. SN - 0939-5075 UR - https://www.unboundmedicine.com/medline/citation/18669035/Transepithelial_transport_and_stability_in_blood_serum_of_angiotensin_I_converting_enzyme_inhibitory_dipeptides_ DB - PRIME DP - Unbound Medicine ER -