Bioavailability of antihypertensive lactoferricin B-derived peptides: Transepithelial transport and resistance to intestinal and plasma peptidases
The transepithelial transport of the angiotensin I-converting enzyme (ACE)-inhibitory and antihypertensive lactoferricin B (LfcinB)-derived hexapeptide LfcinB20-25 (RRWQWR) and of its two main fragments RWQ and WQ were investigated using a human intestinal cell (Caco-2) monolayer. The three peptides were susceptible to the action of brush-border peptidases. Intact LfcinB20-25 was not transported across Caco-2 whereas RWQ and WQ were both absorbed through the cell monolayer. Apparent permeability (Papp) values for absorptive transport across the monolayer were 0.7×10-8cms-1 (RWQ) and 3.9×10-8cms-1 (WQ). The effect of pathway-selective inhibitors on peptide absorption suggested paracellular diffusion as the main mechanism for the transport of intact RWQ and WQ. Invitro incubation in human plasma showed half-life values of 1.9min (RWQ) and 2.3h (WQ). These results highlight the possibility of transport of antihypertensive lactoferricin B-derived peptides across human intestinal mucosa. © 2013 Elsevier Ltd.
| Main Authors: | , , , , , |
|---|---|
| Other Authors: | |
| Format: | artículo biblioteca |
| Published: |
Elsevier
2013
|
| Online Access: | http://hdl.handle.net/10261/99815 http://dx.doi.org/10.13039/501100004587 http://dx.doi.org/10.13039/501100003359 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|