{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T07:41:18Z","timestamp":1791877278599,"version":"4.3.4"},"reference-count":0,"publisher":"African Traditional Herbal Medicine Supporters Initiative (ATHMSI)","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Afr J  Tradit Complement Altern Med"],"abstract":"<jats:p>Background: The commercially available synthetic angiotensin-I-converting enzyme (ACE) inhibitors are known to\r\nexert negative side effects which have driven many research groups globally to discover the novel ACE inhibitors.\r\nMethod: Literature search was performed within the PubMed, ScienceDirect.com and Google Scholar.\r\nResults: The presence of proline at the C-terminal tripeptide of ACE inhibitor can competitively inhibit the ACE\r\nactivity. The effects of other amino acids are less studied leading to difficulties in predicting potent peptide sequences.\r\nThe broad specificity of the enzyme may be due to the dual active sites observed on the somatic ACE. The inhibitors\r\nmay not necessarily competitively inhibit the enzyme which explains why some reported inhibitors do not have the\r\ncommon ACE inhibitor characteristics. Finally, the in vivo assay has to be carried out before the peptides as the\r\nantihypertensive agents can be claimed. The peptides must be absorbed into circulation without being degraded, which\r\nwill affect their bioavailability and potency. Thus, peptides with strong in vitro IC50 values do not necessarily have the\r\nsame effect in vivo and vice versa.\r\nConclusion: The relationship between peptide amino acid sequence and inhibitory activity, in vivo studies of the active\r\npeptides and bioavailability must be studied before the peptides as antihypertensive agents can be claimed.<\/jats:p>","DOI":"10.21010\/ajtcam.v14i2.39","type":"journal-article","created":{"date-parts":[[2017,3,29]],"date-time":"2017-03-29T10:59:47Z","timestamp":1490785187000},"page":"383-406","source":"Crossref","is-referenced-by-count":56,"title":["STRUCTURAL CHARACTERISTICS AND ANTIHYPERTENSIVE EFFECTS OF ANGIOTENSIN-ICONVERTING ENZYME INHIBITORY PEPTIDES IN THE RENIN-ANGIOTENSIN AND KALLIKREIN KININ SYSTEMS"],"prefix":"10.21010","volume":"14","author":[{"given":"Sivananthan","family":"Manoharan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adawiyah Suriza","family":"Shuib","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noorlidah","family":"Abdullah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"8656","published-online":{"date-parts":[[2017,1,13]]},"container-title":["African Journal of Traditional, Complementary and Alternative Medicines"],"original-title":[],"link":[{"URL":"http:\/\/journals.athmsi.org\/index.php\/ajtcam\/article\/download\/4609\/pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/journals.athmsi.org\/index.php\/ajtcam\/article\/download\/4609\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,6]],"date-time":"2023-05-06T09:12:57Z","timestamp":1683364377000},"score":1,"resource":{"primary":{"URL":"http:\/\/journals.athmsi.org\/index.php\/ajtcam\/article\/view\/4609"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,1,13]]},"references-count":0,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2017,1,13]]}},"URL":"https:\/\/doi.org\/10.21010\/ajtcam.v14i2.39","relation":{},"ISSN":["2505-0044","0189-6016"],"issn-type":[{"value":"2505-0044","type":"electronic"},{"value":"0189-6016","type":"print"}],"subject":[],"published":{"date-parts":[[2017,1,13]]}}}