Structural Design of Oligopeptides for Intestinal Transport Model

Seong Min Hong, Mitsuru Tanaka, Riho Koyanagi, Weilin Shen, Toshiro Matsui

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)


Glycyl-sarcosine (Gly-Sar) is a well-known model substrate for the intestinal uptake of dipeptides through peptide transporter 1 (PepT1). However, there are no other model peptides larger than tripeptides to evaluate their intestinal transport ability. In this study, we designed new oligopeptides based on the Gly-Sar structure in terms of protease resistance. Gly-Sar-Sar was found to be an appropriate transport model for tripeptides because it does not degrade during the transport across the rat intestinal membrane, while Gly-Gly-Sar was degraded to Gly-Sar during the 60 min transport. Caco-2 cell transport experiments revealed that the designed oligopeptides based on Gly-Sar-Sar showed a significantly (p < 0.05) lower transport ability by factors of 1/10-, 1/25-, and 1/40-fold for Gly-Sar-Sar, Gly-Sar-Sar-Sar, and Gly-Sar-Sar-Sar-Sar, respectively, compared to Gly-Sar (apparent permeability coefficient: 38.6 ± 11.4 cm/s). Cell experiments also showed that the designed tripeptide and Gly-Sar were transported across Caco-2 cell via PepT1, whereas the tetra- A nd pentapeptides were transported through the paracellular tight-junction pathway.

Original languageEnglish
Pages (from-to)2072-2079
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Issue number10
Publication statusPublished - Mar 16 2016

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)


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