In the early detection of rheumatoid arthritis (RA) synthetic filaggrin peptides serve as antigens for rheumatoid-specific autoantibodies (anti-citrullinated peptide antibody, ACPA) in ELISA tests. In this work we present a peptide that exhibits the binding epitope of ACPA in the form of a stable folding β-hairpin. The homogeneity of the peptide folding was confirmed by NMR spectroscopy and might lead to the first proposed structure of the antibody-bound conformation of the epitope.
Keywords: NMR spectroscopy; disulfides; filaggrin; peptides; β-hairpin.
© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.