title: Filaggrin peptides with β-hairpin structure bind rheumatoid arthritis antibodies.
abstract: 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.
authors.affiliation: Faculty of Chemistry, Philipps University Marburg, Hans-Meerwein-Strasse, 35032 Marburg (Germany).
authors.forename: Sabrina
authors.initials: S
authors.lastname: Fischer
authors.forename: Armin
authors.initials: A
authors.lastname: Geyer
mesh_terms: D001172:Arthritis, Rheumatoid / Q000097:blood* / Q000175:diagnosis* / Q000276:immunology; D001323:Autoantibodies / Q000097:blood*; D000091344:Filaggrin Proteins; D006801:Humans; D007381:Intermediate Filament Proteins / Q000276:immunology* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy
chemical_list: D001323:Autoantibodies; C000717249:FLG protein, human; D000091344:Filaggrin Proteins; D007381:Intermediate Filament Proteins
keywords: NMR spectroscopy; disulfides; filaggrin; peptides; β-hairpin