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Synergistic inhibitory activity of alpha- and beta-LFA-1 peptides on LFA-1/ICAM-1 interaction

H Yusuf-Makagiansar1, I T Makagiansar, Y Hu

  • 1Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, KS 66047, USA.

Peptides
|January 12, 2002
PubMed

Insights

This study reveals that peptide LBE enhances the binding of peptide cLAB.L to cells, improving inhibition of T-cell adherence. LBE modifies ICAM-1 conformation, suggesting a distinct binding site for enhanced LFA-1/ICAM-1 interaction blocking.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Leukocyte function-associated antigen 1 (LFA-1) and its ligand intercellular adhesion molecule 1 (ICAM-1) are crucial for immune and inflammatory processes.
  • Critical binding residues for LFA-1/ICAM-1 interaction are located in the I-domain of LFA-1's alpha-subunit and the I-like domain of its beta-subunit.
  • Previous research identified the cyclic peptide cLAB.L, derived from the LFA-1 I-domain, as an inhibitor of LFA-1/ICAM-1 interaction.

Purpose of the Study:

  • To investigate the effect of the I-like domain peptide LBE on the binding mechanism of the LFA-1 inhibitor cLAB.L.
  • To elucidate the roles of LBE and cLAB.L in modulating LFA-1/ICAM-1 interactions and T-cell adherence.
  • To understand how LBE influences ICAM-1 conformation and its subsequent binding with cLAB.L.

Main Methods:

  • Utilized T-cells and epithelial cells to study cell adhesion.
  • Administered peptides cLAB.L and LBE in varying sequences to assess their impact on cell adherence.
  • Analyzed ICAM-1 conformation changes induced by peptide treatment.

Main Results:

  • Peptide LBE was found to enhance the binding of peptide cLAB.L to both T-cells and epithelial cells.
  • The combined application of LBE and cLAB.L significantly suppressed the adherence of T-cells to epithelial monolayers.
  • Pre-treatment of epithelial monolayers with LBE before adding cLAB.L yielded a superior inhibitory effect compared to the reverse order.
  • LBE induced conformational changes in ICAM-1, distinct from cLAB.L's binding site, facilitating enhanced cLAB.L binding.

Conclusions:

  • Peptide LBE acts synergistically with cLAB.L to inhibit LFA-1/ICAM-1-mediated T-cell adherence.
  • LBE's ability to alter ICAM-1 conformation is key to enhancing the inhibitory efficacy of cLAB.L.
  • This study provides insights into novel strategies for modulating immune cell interactions through combined peptide therapies targeting LFA-1 and ICAM-1.

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