Tryptophan-containing dipeptides are C-domain selective inhibitors of angiotensin converting enzyme
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
Somatic angiotensin-converting enzyme (ACE) contains two active sites, the C- and N-domain, from which the C-domain is supposed to play a major role in blood pressure regulation and is therefore a promising pharmacological target to reduce blood pressure without side-effects. We report for the first time that tryptophan-containing dipeptides such as Ile-Trp or Val-Trp, which were recently found in food protein hydrolysates, are selective and competitive inhibitors for the C-domain with a selectivity factor of 40 and 70, respectively. Structure-activity studies showed that an N-terminal aliphatic amino acid and a tryptophan moiety in the P2' position are favourable structures for C-domain inhibition in dipeptides. In contrast, the lactotripeptides Ile-Pro-Pro and Val-Pro-Pro, which were widely used as ingredients for hypotensive food, showed a slight selectivity for the N-domain. Hence, tryptophan containing dipeptides are interesting ingredients for functional foods as a natural prevention for hypertension with reduced side effects due to its selective inhibition of the C-domain. (C) 2014 Elsevier Ltd. All rights reserved.
Details
Original language | English |
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Pages (from-to) | 596-602 |
Number of pages | 7 |
Journal | Food Chemistry |
Volume | 166 |
Publication status | Published - 1 Jan 2015 |
Peer-reviewed | Yes |
External IDs
Scopus | 84904012978 |
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WOS | 000342654200080 |
Keywords
Keywords
- Angiotensin converting enzyme (ACE), Domain selective inhibitors, Bioactive peptides, Tryptophan peptides, 2 HOMOLOGOUS DOMAINS, BLOOD-PRESSURE, ACTIVE-SITES, N-DOMAIN, SPECIFICITY, BRADYKININ, PEPTIDES, SUBSTRATE, CLEAVAGE