Faculty of Chemistry, Philipps University Marburg, Hans-Meerwein-Strasse, 35032 Marburg (Germany).
Angew Chem Int Ed Engl. 2014 Apr 7;53(15):3849-53. doi: 10.1002/anie.201309873. Epub 2014 Mar 5.
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.
在类风湿关节炎（RA）的早期检测中，合成的丝聚蛋白肽在 ELISA 试验中作为类风湿相关自身抗体（抗瓜氨酸化肽抗体，ACPA）的抗原。在这项工作中，我们展示了一种以稳定折叠 β-发夹形式呈现 ACPA 结合表位的肽。通过 NMR 光谱证实了该肽折叠的均一性，这可能导致首次提出该表位与抗体结合的构象结构。
