During this thesis filaggrin peptides with a defined conformation in solution were synthesized and analyzed. Filaggrin peptides have a biologically active peptide sequence which is able to recognize autoantibodies formed in a disease with rheumatoid arthritis. The structure of the rigid filaggrin peptides was elucidated by NMR spectroscopy and their influence on the biological activity was analyzed by immunoassays. Amino acid mimetics provided information about the position and properties of the binding epitope and the effects of amino acids and functionalities on the folding of the peptide. Thus a crucial contribution to the elucidation of the geometry of the epitope-antibody binding and to the development of a personalized diagnosis of rheumatiod arthritis based on immunoassays has been done.
