Synergistic inhibitory activity of alpha- and beta-LFA-1 peptides on LFA-1/ICAM-1 interaction.
Interactions of cell-adhesion molecule LFA-1 and its ligand ICAM-1 play important roles during immune and inflammatory responses. Critical residues of LFA-1 for ICAM-1 binding are known to be in the I-domain of the alpha-subunit and the I-like domain of the beta-subunit. On the basis of our previous work demonstrating the ... inhibitory activity of I-domain cyclic peptide cLAB.L on LFA-1/ICAM-1 interaction, here we have explored the activity of I-like-domain peptide LBE on the binding mechanism of cLAB.L. LBE enhances cLAB.L binding to T-cells and epithelial cells. The adherence of T-cells to epithelial monolayers was suppressed by the two peptides. The addition of LBE to the monolayers prior to the addition cLAB.L produced a better inhibitory effect than the reverse procedure. LBE, but not cLAB.L, changes the ICAM-1 conformation, suggesting that LBE binds to ICAM-1 at sites that are distinct from these of cLAB.L and induces improved conformation in ICAM-1 for binding to cLAB.L.
Mesh Terms:
Caco-2 Cells, Cell Line, Humans, Intercellular Adhesion Molecule-1, Lymphocyte Function-Associated Antigen-1, Lymphocytes, Peptide Fragments, Protein Binding, Protein Conformation, Spectrometry, Fluorescence
Caco-2 Cells, Cell Line, Humans, Intercellular Adhesion Molecule-1, Lymphocyte Function-Associated Antigen-1, Lymphocytes, Peptide Fragments, Protein Binding, Protein Conformation, Spectrometry, Fluorescence
Peptides
Date: Dec. 01, 2001
PubMed ID: 11786177
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