Advanced search
1 file | 847.39 KB

Bioavailability of angiotensin I converting enzyme inhibitory peptides

(2004) BRITISH JOURNAL OF NUTRITION. 92(3). p.357-366
Author
Organization
Abstract
Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo 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.
Keywords
FOOD PROTEINS, ANTIHYPERTENSIVE PEPTIDE, BLOOD-PRESSURE, BIOACTIVE PEPTIDES, HIS-ILE-ARG, HUMAN INTESTINAL-CELL, SPONTANEOUSLY HYPERTENSIVE-RATS, intestinal transport, gastrointestinal digestion, bioactive peptides, hypertension, TRANSEPITHELIAL TRANSPORT, LACTOBACILLUS-CASEI, MILK-PROTEINS

Downloads

  • (...).pdf
    • full text
    • |
    • UGent only
    • |
    • PDF
    • |
    • 847.39 KB

Citation

Please use this url to cite or link to this publication:

Chicago
Vermeirssen, Vanessa, John Van Camp, and Willy Verstraete. 2004. “Bioavailability of Angiotensin I Converting Enzyme Inhibitory Peptides.” British Journal of Nutrition 92 (3): 357–366.
APA
Vermeirssen, Vanessa, Van Camp, J., & Verstraete, W. (2004). Bioavailability of angiotensin I converting enzyme inhibitory peptides. BRITISH JOURNAL OF NUTRITION, 92(3), 357–366.
Vancouver
1.
Vermeirssen V, Van Camp J, Verstraete W. Bioavailability of angiotensin I converting enzyme inhibitory peptides. BRITISH JOURNAL OF NUTRITION. 2004;92(3):357–66.
MLA
Vermeirssen, Vanessa, John Van Camp, and Willy Verstraete. “Bioavailability of Angiotensin I Converting Enzyme Inhibitory Peptides.” BRITISH JOURNAL OF NUTRITION 92.3 (2004): 357–366. Print.
@article{300064,
  abstract     = {Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo 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.},
  author       = {Vermeirssen, Vanessa and Van Camp, John and Verstraete, Willy},
  issn         = {0007-1145},
  journal      = {BRITISH JOURNAL OF NUTRITION},
  keyword      = {FOOD PROTEINS,ANTIHYPERTENSIVE PEPTIDE,BLOOD-PRESSURE,BIOACTIVE PEPTIDES,HIS-ILE-ARG,HUMAN INTESTINAL-CELL,SPONTANEOUSLY HYPERTENSIVE-RATS,intestinal transport,gastrointestinal digestion,bioactive peptides,hypertension,TRANSEPITHELIAL TRANSPORT,LACTOBACILLUS-CASEI,MILK-PROTEINS},
  language     = {eng},
  number       = {3},
  pages        = {357--366},
  title        = {Bioavailability of angiotensin I converting enzyme inhibitory peptides},
  url          = {http://dx.doi.org/10.1079/BJN20041189},
  volume       = {92},
  year         = {2004},
}

Altmetric
View in Altmetric
Web of Science
Times cited: