4.1 Article

Impact of peptide permeation enhancer on tight junctions opening cellular mechanisms

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DOI: 10.1016/j.bbrep.2022.101375

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Tight junction; PKC zeta; L -R5 peptide; Occludin; Protein interaction

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This study demonstrates that L-R5 interacts directly with TJ proteins, preventing the binding and phosphorylation of occludin by PKC zeta, resulting in TJ disruption and enhanced epithelial permeability.
The myristoylated pentapeptide, L-R5, contains an amino acid sequence of the zeta inhibitory peptide (ZIP) portion (pseudosubstrate) of protein kinase C zeta (PKC zeta). As PKC zeta is involved in the modulation of epithelial tight junctions (TJs) through the phosphorylation of TJ proteins, L-R5 was suggested to interact with the enzyme resulting in the enhancement of paracellular permeability. This study shows that L-R5 does not bind to the enzyme but interacts directly with TJ proteins. We show here that the binding of PKC zeta to occludin and its successive phosphorylation is prevented by L-R5, which leads to TJ disruption and enhanced epithelial permeability. Although L-R5 did not show any in vitro cytotoxicity, a proteomics study revealed that L-R5 interferes with other regulatory pathways, e.g., apoptosis and immune response. We suggest that structural modification of the peptide may increase the specificity TJ protein-peptide interaction.

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