| Abstract
| - Sera from patients suffering from autoimmune disorders often contain multiple types of autoantibodies,some of which can be exclusive of a disease and thus used as biomarkers for diagnosis. Identification ofthese autoantibodies, as disease biomarkers, should be achieved using native antigens in simple biologicalassays. However, posttranslational modifications, such as glycosylation, may play a fundamental role forspecific autoantibody recognition. In line with these observations, we described synthetic glycopeptidesable to detect high autoantibody titers in sera of patients affected by multiple sclerosis, an inflammatory,demyelinating disease of the central nervous system. We describe here the conformation−activity relationshipof a focused library of glycopeptides based on structural diversity, with the aim of defining the structuralrequirements for the interaction of these glycopeptide antigens with specific autoantibodies. The final goalis the optimization of an antigenic probe for multiple sclerosis, to be used in the development of a simplediagnostic test based on an immunoenzymatic assay. The reported results clearly indicate that glycopeptidesable to reveal high antibody titers in multiple sclerosis sera are characterized by a type I‘ β-turn around theminimal epitope Asn(Glc), which allows an efficient exposure of this moiety to antibodies interactions, inthe context of a solid-phase immunoenzymatic assay.
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