Format

Send to

Choose Destination
See comment in PubMed Commons below
J Enzyme Inhib Med Chem. 2003 Oct;18(5):407-12.

Characterization of new milk-derived inhibitors of angiotensin converting enzyme in vitro and in vivo.

Author information

  • 1Danish University of Pharmaceutical Science, Department of Pharmacology, Universitetsparken 2, DK-2100 Copenhagen O, Denmark. anfu@dfh.dk

Abstract

Inhibition of angiotensin converting enzyme (ACE) has been observed with a variety of different peptides, and peptide fragments with inhibitory capabilities have been identified within many different proteins, including milk proteins. The purpose of this study therefore was to identify new short peptides with inhibitory properties from the primary structure of milk proteins and to characterize them in vitro and in vivo, since no milk derived ACE inhibitors have previously been evaluated for their ability to inhibit ACE in vivo. In vitro, 8 of 9 dipeptides were found to be competitive inhibitors of ACE. The IC50 was significantly lower when an angiotensin I-like substrate was used, than when a bradykinin-like substrate was used. Using three different in vivo models for ACE inhibition, a very moderate effect was observed for three of the new peptides, but only for up to 6 or 12 minutes. Nothing was observed with two reference compounds that are reported to be hypotensive ACE-inhibitors derived from milk proteins. This raises the question whether the mechanism of hypotensive action is straightforward inhibition of ACE in vivo.

PMID:
14692507
DOI:
10.1080/1475636031000138723
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Taylor & Francis
    Loading ...
    Support Center