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STRUCTURAL CHARACTERISTICS AND ANTIHYPERTENSIVE EFFECTS OF ANGIOTENSIN-ICONVERTING ENZYME INHIBITORY PEPTIDES IN THE RENIN-ANGIOTENSIN AND KALLIKREIN KININ SYSTEMS
Background: The commercially available synthetic angiotensin-I-converting enzyme (ACE) inhibitors are known to exert negative side effects which have driven many research groups globally to discover the novel ACE inhibitors. Method: Literature search was performed within the PubMed, ScienceDirect.co...
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Published in: | African journal of traditional, complementary, and alternative medicines complementary, and alternative medicines, 2017-01, Vol.14 (2), p.383-406 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Citations: | Items that cite this one |
Online Access: | Get full text |
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Summary: | Background: The commercially available synthetic angiotensin-I-converting enzyme (ACE) inhibitors are known to
exert negative side effects which have driven many research groups globally to discover the novel ACE inhibitors.
Method: Literature search was performed within the PubMed, ScienceDirect.com and Google Scholar.
Results: The presence of proline at the C-terminal tripeptide of ACE inhibitor can competitively inhibit the ACE
activity. The effects of other amino acids are less studied leading to difficulties in predicting potent peptide sequences.
The broad specificity of the enzyme may be due to the dual active sites observed on the somatic ACE. The inhibitors
may not necessarily competitively inhibit the enzyme which explains why some reported inhibitors do not have the
common ACE inhibitor characteristics. Finally, the in vivo assay has to be carried out before the peptides as the
antihypertensive agents can be claimed. The peptides must be absorbed into circulation without being degraded, which
will affect their bioavailability and potency. Thus, peptides with strong in vitro IC50 values do not necessarily have the
same effect in vivo and vice versa.
Conclusion: The relationship between peptide amino acid sequence and inhibitory activity, in vivo studies of the active
peptides and bioavailability must be studied before the peptides as antihypertensive agents can be claimed. |
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ISSN: | 0189-6016 2505-0044 |
DOI: | 10.21010/ajtcam.v14i2.39 |