Over the last years, our research has focused on discovery, engineering, and synthesis of ultra stable peptides with the overall aim to find applications in biotechnology and medicine (1,2). Currently, we capitalize on such scaffold peptides in the development of a new strategy for diagnosis and treatment of autoimmune diseases: neutralization of pathogenic autoantibodies using peptide blockers (3).
Rheumatoid arthritis is an autoimmune disease, which is characterized by chronic inflammation, destruction of joints, and pain. The aetiology of the disease is still unclear, but a major part—60 to 70%— of persons suffering of rheumatoid arthritis carry autoantibodies against citrullinated proteins. In fact, the presence of anti-citrullinated protein/peptide antibodies (ACPAs) is one of the specific serological diagnostic markers of the disease. ACPAs emerge as an immune response towards proteins containing citrulline, which are the results of specific enzymes, peptidylarginine deiminases, converting arginine to citrulline.
We have shown that short peptide blockers are able to neutralize ACPAs (4). These peptide blockers are based on the discovery of specific citrullinated protein sequences that trigger autoimmune responses, which then are incorporated into the peptide scaffolds to improve stability and binding properties.