Transepithelial transport of dry-cured ham peptides with ACE inhibitory activity through a Caco-2 cell monolayer
Marta Gallego and colleagues from the Instituto de Agroquímica y Tecnología de Alimentos (CSIC, ES) and the Ghent University (BE) have examined the stability of naturally occurring angiotensin converting enzyme (ACE)-inhibitors in dry-cured ham during intestinal trans-epithelial transport using a Caco-2 cell monolayer model system.
Previous studies have shown that dry-cured ham is an important source of naturally generated bioactive peptides including those with ACE-inhibitor activity. However, it is not clear whether these compounds resist intestinal degradation and reach the blood stream intact. This study demonstrates the potential for intact dry-cured ham peptides, as well as their fragments, to cross the intestinal epithelium and reach the blood stream where they may exert an antihypertensive action.
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- Peptides AAATP, AAPLAP, and KKPVAAP were hydrolysed during transport across the Caco-2-cell monolayer, although KPVAAP was also absorbed intact.
- This study provides evidence for the absorption and generation of ACE-inhibitory peptide fragments originating from dry-cured ham.
- ACE-inhibitor activity of the peptides or associated fragments suggests that dry-cured ham peptides could reach the circulatory system to exert an antihypertensive action.