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Discovery and structure-activity relationships of small molecules that block the human immunoglobulin G-human neonatal Fc receptor (hIgG-hFcRn) protein-protein interaction.

Abstract
The neonatal Fc receptor, FcRn, prolongs the half-life of IgG in the serum and represents a potential therapeutic target for the treatment of autoimmune disease. Small molecules that block the protein-protein interactions of human IgG-human FcRn may lower pathogenic autoantibodies and provide effective treatment. A novel class of quinoxalines has been discovered as antagonists of the IgG:FcRn protein-protein interaction through optimization of a hit derived from a virtual ligand-based screen.
AuthorsZhaolin Wang, Cara Fraley, Adam R Mezo
JournalBioorganic & medicinal chemistry letters (Bioorg Med Chem Lett) Vol. 23 Issue 5 Pg. 1253-6 (Mar 1 2013) ISSN: 1464-3405 [Electronic] England
PMID23375228 (Publication Type: Journal Article)
CopyrightCopyright © 2013 Elsevier Ltd. All rights reserved.
Chemical References
  • Fc receptor, neonatal
  • Histocompatibility Antigens Class I
  • Immunoglobulin G
  • Ligands
  • Quinoxalines
  • Receptors, Fc
Topics
  • Drug Evaluation, Preclinical
  • Histocompatibility Antigens Class I (immunology, metabolism)
  • Humans
  • Immunoglobulin G (immunology, metabolism)
  • Ligands
  • Protein Interaction Domains and Motifs (drug effects)
  • Quinoxalines (pharmacology)
  • Receptors, Fc (antagonists & inhibitors, immunology, metabolism)
  • Structure-Activity Relationship

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