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Transport of ACE Inhibitory Peptides Ile-Gln-Pro and Val-Glu-Pro Derived from Spirulina platensis Across Caco-2 Monolayers.

This study evaluated transepithelial transport mechanisms of Ile-Gln-Pro (IQP) and Val-Glu-Pro (VEP), two ACE-inhibitory peptides derived from Spirulina platensis, using human intestinal Caco-2 cell monolayers. IQP and VEP were absorbed intact through Caco-2 cell monolayers with Papp values of 7.48 ± 0.58 × 10-6 and 5.05 ± 0.74 × 10-6 cm/s, respectively. The transport of IQP and VEP were affected neither by Gly-Pro nor by wortmannin, indicating that they were not PepT1-mediated and did not involve endocytosis. However, transport of IQP and VEP were increased significantly by sodium deoxycholate, suggesting that the major transport mechanism was paracellular. In addition, the increased transport of VEP and IQP were followed with the addition of sodium azide, suggesting influence of energy to the process. The transport of VEP was also increased by verapamil, indicating an apical-to-basolateral flux mediated by P-gp.


PRACTICAL APPLICATION
Bioactive peptides derived from food proteins have been considered as potentially ideal products to reduce hypertension because of their safety and positive impacts on health. IQP and VEP are the 2 ACE inhibitory peptides derived from Spirulina platensis, a kind of edible cyanobacteria with rich nutrition and multiple physiological functions, and were demonstrated to inhibit ACE and lower blood pressure in spontaneously hypertensive rats. However, it is prerequisite that such bioactive peptides must be absorbed intact across the intestinal epithelium, so as to exert antihypertensive effects in vivo. This study evaluated transepithelial transport mechanisms of IQP and VEP. It contributes to the study of Spirulina in lowering blood pressure and supports the development of bioactive peptide products.