Journal article

Structure based design and characterization of peptides that inhibit IgE binding to its high-affinity receptor

JM McDonnell, AJ Beavil, GA Mackay, BA Jameson, R Korngold, HJ Gould, BJ Sutton

NATURE STRUCTURAL BIOLOGY | NATURE PUBLISHING GROUP | Published : 1996

Abstract

We have designed synthetic peptide inhibitors of the interaction between IgE and its high affinity receptor, Fc epsilon RI. The structure of the second domain of CD2 was used as a modelling template for the second alpha-chain domain of Fc epsilon RI, the C-C' loop of which has been implicated in the interaction with IgE. An L-amino acid peptide and a retro-enantiomeric D-amino acid peptide were designed to mimic the conformation of the C-C' region. Both peptides were cyclized by disulphide bond formation between terminal cysteine residues, and show mirror image symmetry by circular dichroism analysis. The C-C' peptide mimics act as competitive inhibitors of IgE binding. The cyclic L- and ret..

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University of Melbourne Researchers