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An ACE inhibitory activity<jats:italic>in vitro<\/jats:italic>does not always imply an antihypertensive effect<jats:italic>in vivo<\/jats:italic>. Even if it does, it is very difficult to establish a direct relationship between<jats:italic>in vitro<\/jats:italic>and<jats:italic>in vivo<\/jats:italic>activity. This is mainly due to the bioavailability of the ACE inhibitory peptides after oral administration and the fact that peptides may influence blood pressure by mechanisms other than ACE inhibition. To exert an antihypertensive effect after oral ingestion, ACE inhibitory peptides have to reach the cardiovascular system in an active form. Therefore, they need to remain active during digestion by human proteases and be transported through the intestinal wall into the blood. The bioavailability of some ACE inhibitory peptides has been studied. It is also known that (hydroxy)proline-containing peptides are generally resistant to degradation by digestive enzymes. Peptides can be absorbed intact through the intestine by paracellular and transcellular routes, but the potency of the bioactivity after absorption is inversely correlated to chain length. In addition, some strategies are proposed to increase the bioavailability of ACE inhibitory peptides. Further research into the bioavailability of ACE inhibitory peptides will lead to the development of more effective ACE inhibitory peptides and foods.<\/jats:p>","DOI":"10.1079\/bjn20041189","type":"journal-article","created":{"date-parts":[[2004,10,7]],"date-time":"2004-10-07T22:12:20Z","timestamp":1097187140000},"page":"357-366","source":"Crossref","is-referenced-by-count":465,"title":["Bioavailability of angiotensin I converting enzyme inhibitory peptides"],"prefix":"10.1017","volume":"92","author":[{"given":"Vanessa","family":"Vermeirssen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John Van","family":"Camp","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Willy","family":"Verstraete","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"56","published-online":{"date-parts":[[2007,3,9]]},"reference":[{"key":"S0007114504001801_ref088","doi-asserted-by":"publisher","DOI":"10.3168\/jds.S0022-0302(99)75364-6"},{"key":"S0007114504001801_ref052","doi-asserted-by":"publisher","DOI":"10.1016\/S0024-3205(00)00471-9"},{"key":"S0007114504001801_ref002","doi-asserted-by":"publisher","DOI":"10.1016\/0006-2952(71)90292-9"},{"key":"S0007114504001801_ref063","doi-asserted-by":"publisher","DOI":"10.1093\/ajcn\/77.2.326"},{"key":"S0007114504001801_ref087","doi-asserted-by":"publisher","DOI":"10.2174\/1381612033454801"},{"key":"S0007114504001801_ref037","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1099-1387(199907)5:7<289::AID-PSC196>3.0.CO;2-6"},{"key":"S0007114504001801_ref021","volume-title":"Transmucosal passage of intact peptides","author":"Gardner","year":"1998"},{"key":"S0007114504001801_ref093","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0029(20000515)49:4<346::AID-JEMT3>3.0.CO;2-B"},{"key":"S0007114504001801_ref090","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/S0008-6363(98)00077-7","article-title":"Lessons from rat models of hypertension: from Goldblatt to genetic engineering","volume":"39","author":"Yigal","year":"1998","journal-title":"Cardiovasc Res"},{"key":"S0007114504001801_ref086","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0282(1997)43:2<129::AID-BIP5>3.0.CO;2-X"},{"key":"S0007114504001801_ref017","first-page":"456","volume-title":"Protein digestion and assimilation","author":"Ganapathy","year":"1999"},{"key":"S0007114504001801_ref041","doi-asserted-by":"publisher","DOI":"10.1016\/S0167-7799(00)01439-6"},{"key":"S0007114504001801_ref089","doi-asserted-by":"publisher","DOI":"10.1023\/A:1018982505021"},{"key":"S0007114504001801_ref073","unstructured":"Tome D (1998) Functional peptides. 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