1. 2,4,6-trisubstituted triazines as protein a mimetics for the treatment of autoimmune diseases
- Author
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Brigitte Grouix, Boulos Zacharie, Shaun D. Abbott, Dannyck Gaudreau, Jean-Simon Duceppe, Marie-Eve Fafard, Abdallah Ezzitouni, Lyne Gagnon, François Sarra-Bournet, Natalie St-Amant, Caroline Lauzon, Nancie Moreau, Valérie Perron, Alan D. Cameron, Christopher Penney, Nicole Wilb, Jean-François Bienvenu, André Doucet, Michel Asselin, Daniel Fortin, Karine Houde, and Josée Cloutier
- Subjects
Models, Molecular ,Protein Conformation ,Enzyme-Linked Immunosorbent Assay ,Kidney ,Chemical synthesis ,Immunoglobulin G ,Mice ,Structure-Activity Relationship ,Protein structure ,Biomimetic Materials ,Drug Discovery ,medicine ,Structure–activity relationship ,Animals ,Humans ,Lupus Erythematosus, Systemic ,Staphylococcal Protein A ,chemistry.chemical_classification ,Autoimmune disease ,biology ,Molecular Structure ,Chemistry ,Triazines ,medicine.disease ,Biochemistry ,Antibodies, Antinuclear ,biology.protein ,Molecular Medicine ,Antibody ,Glycoprotein ,Protein A - Abstract
A first-in-class series of low molecular weight trisubstituted triazines were synthesized and evaluated for their ability to mimic protein A binding to human IgG antibody. The structure-activity relationship (SAR) demonstrates that the 1,3-phenylenediamine component was essential for robust activity. Twenty-two compounds, represented by lead molecule 34, displayed significant activity compared to protein A. These compounds may prove useful for the treatment of autoimmune disease.
- Published
- 2010