Ala-Val-Phe and Val-Phe: ACE inhibitory peptides derived from insect protein with antihypertensive activity in spontaneously hypertensive rats
| Autor: | Nicole Morel, John Van Camp, Guy Smagghe, Pierre Rougé, Lieselot Vercruysse, Griet Herregods |
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| Rok vydání: | 2009 |
| Předmět: |
medicine.medical_specialty
Physiology Peptide Angiotensin-Converting Enzyme Inhibitors Blood Pressure Tripeptide Biology Peptidyl-Dipeptidase A Biochemistry Cellular and Molecular Neuroscience Endocrinology Oral administration In vivo Internal medicine Rats Inbred SHR medicine Animals Humans Antihypertensive Agents chemistry.chemical_classification Protein Stability Captopril Angiotensin-converting enzyme In vitro Rats Enzyme Activation chemistry ACE inhibitor biology.protein Insect Proteins Peptides medicine.drug |
| Zdroj: | Peptides. 31(3) |
| ISSN: | 1873-5169 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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