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Stabilized cyclic peptides as scavengers of autoantibodies: neutralization of anti-citrullinated protein/peptide antibodies in rheumatoid arthritis.

08:00 EDT 9th April 2018 | BioPortfolio

Summary of "Stabilized cyclic peptides as scavengers of autoantibodies: neutralization of anti-citrullinated protein/peptide antibodies in rheumatoid arthritis."

The occurrence of autoantibodies is a hallmark of rheumatoid arthritis, specifically those autoantibodies targeting proteins containing the arginine derived amino acid citrulline. There is strong evidence showing that the occurrence of anti-citrullinated protein/peptide antibodies (ACPA) are involved in disease progression, and ACPA was recently shown to induce pain in animals. Here, we explore a novel concept useful for research, diagnostics, and possibly therapy of autoimmune diseases, namely to directly target and neutralize autoantibodies using peptide binders. A high affinity peptide based scavenger of ACPA was developed by grafting a citrullinated epitope derived from human fibrinogen into a naturally occurring stable peptide scaffold. The best scavenger comprises the truncated epitope α-fibrinogen, [Cit573]fib(566-580), grafted into the scaffold sunflower trypsin inhibitor-1, SFTI-1. The final peptide demonstrates low nanomolar apparent affinity and superior stability.

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This article was published in the following journal.

Name: ACS chemical biology
ISSN: 1554-8937
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Medical and Biotech [MESH] Definitions

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