Journal
INTERNATIONAL DAIRY JOURNAL
Volume 32, Issue 2, Pages 169-174Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.idairyj.2013.05.009
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Funding
- Ministerio de Educacion y Ciencia - FEDER [AGL2010-21009, AGL2011-24643]
- Consolider Ingenio
- Fun-C-Food
- Instituto de Salud Carlos III [RETICS RD06/0026/0006]
- Generalitat Valenciana [ACOMP/2012/011]
- Ministerio de Educacion y Ciencia [BES-2008-004472]
- [CSD2007-00063]
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The transepithelial transport of the angiotensin I-converting enzyme (ACE)-inhibitory and antihypertensive lactoferricin B (LfcinB)-derived hexapeptide LfcinB(20-25) (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 LfcinB(20-25) was not transported across Caco-2 whereas RWQ and WQ were both absorbed through the cell monolayer. Apparent permeability (P-app) values for absorptive transport across the monolayer were 0.7 x 10(-8) cm s(-1) (RWQ) and 3.9 x 10(-8) cm s(-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. In vitro incubation in human plasma showed half-life values of 1.9 min (RWQ) and 2.3 h (WQ). These results highlight the possibility of transport of antihypertensive lactoferricin B-derived peptides across human intestinal mucosa. (C) 2013 Elsevier Ltd. All rights reserved.
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