期刊
PEPTIDES
卷 31, 期 3, 页码 482-488出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2009.05.029
关键词
Bioactive peptides; In vitro; Organ baths/rat aorta; In vivo; Bioavailability/stability
资金
- Institute for the Promotion and Innovation by Science and Technology in Flanders (IWT)
- Special Research Fund of the Ghent University [01102703]
- CNRS
In this study, we evaluated the stability/bioavailability and in vivo antihypertensive activity of the tripeptide, Ala-Val-Phe, that was recently purified from insect protein (Spodoptera littoralis; Lepidoptera) and that showed in vitro angiotensin converting enzyme (ACE) inhibitory activity. This tripeptide is partly hydrolyzed by mucosal peptidases to Val-Phe, a more potent in vitro ACE inhibitor. In organ bath experiments using rat aorta, Val-Phe showed ACE inhibition, while Ala-Val-Phe did not. Single oral administration (5 mg/kg body weight) to spontaneously hypertensive rats led to a significant decrease in blood pressure for both peptides. Docking experiments indicated an active character for Val-Phe and an inactive character for Ala-Val-Phe as potential inhibitors of human ACE. From our results, it can be suggested that after oral administration of Ala-Val-Phe, Val-Phe is released by in vivo peptidases and is responsible for in vivo activity of Ala-Val-Phe. To the best of our knowledge this is the first report of in vivo antihypertensive activity of peptides derived from insect protein. (C) 2009 Elsevier Inc. All rights reserved.
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