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Importance of Terminal Amino Acid Residues to the Transport of Oligopeptides across the Caco-2 Cell Monolayer.

The objective of this paper was to investigate the effects of terminal amino acids on the transport of oligopeptides across the Caco-2 cell monolayer. Ala-based tetra- and pentapeptides were designed, and the N- or C-terminal amino acid residues were replaced by different amino acids. The results showed that the oligopeptides had a wide range of transport permeability across the Caco-2 cell monolayer and could be divided into four categories: non-/poor permeability, low permeability, intermediate permeability, and good permeability. Tetrapeptides with N-terminal Leu, Pro, Ile, Cys, Met, and Val or C-terminal Val showed the highest permeability, with apparent permeability coefficient (Papp) values over 10 × 10-6 cm/s (p < 0.05), suggesting that nonpolar hydrophobic aliphatic amino acids or polar sulfur-containing amino acids were the best for the transport of tetrapeptides. Pentapeptides with N- or C-terminal Tyr also showed high permeability levels, with Papp values of about 10 × 10-6 cm/s. The amino acids Glu, Asn, and Thr at the N terminus or Lys, Asp, and Arg at the C terminus were also beneficial for the transport of tetra- and pentapeptides, with Papp values ranging from 1 × 10-6 to 10 × 10-6 cm/s. In addition, peptides with amino acids replaced at the N terminus generally showed higher permeability than those with amino acids replaced at the C terminus (p < 0.05), suggesting that N-terminal amino acids were more important for the transport of oligopeptides across the Caco-2 cell monolayer.