Author: ["Xin Zhang","Dominique Piatier-Tonneau","Charles Auffray","Ramachandran Murali","Ajit Mahapatra","Fuqing Zhang","Curtis C. Maier","H. Saragovi","Mark I. Greene"]
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Abstract
We have developed peptide analogs to analyze precise human CD4 substructures involved in MHC class II binding. Forms of the complementarity determining-like regions (CDRs) of the D1 domain of human CD4 were reproduced as synthetic aromatically modified exocyclic (AME) analogs and tested for their ability to block CD4-MHC II interactions and T cell activation. The exocyclic derived from CDRS (residues 82-89) of human CD4, which specifically associated with CD4 on the T cell surface to create a heteromeric CD4 complex, blocked IL-2 production and antagonized the normal function of the CD4 receptor. The approach of creating novel synthetic antagonistic receptor complexes may represent a new receptor specific pharmaceutical approach to modulate biological function.Cite this article
Zhang, X., Piatier-Tonneau, D., Auffray, C. et al. Synthetic CD4 exocyclic peptides antagonize CD4 holoreceptor binding and T cell activation. Nat Biotechnol 14, 472–475 (1996). https://doi.org/10.1038/nbt0496-472 