期刊
MOLECULAR NUTRITION & FOOD RESEARCH
卷 54, 期 10, 页码 1428-1435出版社
WILEY
DOI: 10.1002/mnfr.200900443
关键词
Caco2-cells; Immunomodulatory peptide; Intestinal transport; Mass spectrometry
Although the bioavailability of large peptides with biological activity is of great interest, the intestinal transport has been described for peptides up to only nine residues. beta-casein (beta-CN, 193-209) is a long and hydrophobic peptide composed of 17 amino acid residues (molecular mass 1881 Da) with immunomodulatory activity. The present work examined the transport of the beta-CN (193-209) peptide across Caco-2 cell monolayer. In addition, we evaluated the possible routes of the beta-CN (193-209) peptide transport, using selective inhibitors of the different routes for peptide transfer through the intestinal barrier. The results showed that the beta-CN (193-209) peptide resisted the action of brush-border membrane peptidases, and that it was transported through the Caco-2 cell monolayer. The main route involved in transepithelial transport of the beta-CN (193-209) peptide was transcytosis via internalized vesicles, although the paracellular transport via tight-junctions could not be excluded. Our results demonstrated the transport of an intact long-chain bioactive peptide in an in vitro model of intestinal epithelium, as an important step to prove the evidence for bioavailability of this peptide.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据