Designed glycopeptides with different beta-turn types as synthetic probes for the detection of autoantibodies as biomarkers of multiple sclerosis

Journal of Medicinal Chemistry
Alfonso CarotenutoPaolo Rovero

Abstract

Circulating autoantibodies have been recognized as disease biomarkers of autoimmune diseases. We have previously disclosed a synthetic glycopeptide that is able to detect specific autoantibodies in sera of patients who are affected by multiple sclerosis (MS). This glycopeptide is characterized by a type I' beta-turn around the minimal epitope Asn(Glc) that allows an efficient exposure of this moiety to antibody interactions in the context of a solid-phase immunoenzymatic assay. With the aim of optimizing the glycopeptide-antibody interactions, we analyze a series of new glycopeptides based on different turn structures. Our results confirm the role of conformation in the recognition and binding of synthetic antigenic probes to MS autoantibodies. Glycopeptide 2, which is characterized by a type I beta-turn around the minimal epitope Asn(Glc), shows the highest antibody affinity (IC50 = 11.8 nM), and thus it appears to be a promising tool for the detection of specific autoantibodies as MS biomarker in patients' sera.

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Citations

Jun 8, 2013·Amino Acids·Alessandro GoriGiorgio Colombo
Oct 1, 2013·European Journal of Medicinal Chemistry·Alfonso CarotenutoPietro Campiglia
Jul 11, 2012·Sensors·Feliciana Real-FernándezPaolo Rovero
Jan 6, 2016·Journal of the American Society for Mass Spectrometry·Chiara GiangrandeJoëlle Vinh
Mar 31, 2015·Journal of Peptide Science : an Official Publication of the European Peptide Society·Cédric RentierAnna Maria Papini
Aug 29, 2009·Journal of Peptide Science : an Official Publication of the European Peptide Society·Anna Maria Papini
Oct 21, 2011·Chemical Society Reviews·Søren L PedersenKnud J Jensen
Mar 23, 2013·Chembiochem : a European Journal of Chemical Biology·Paola FrancoMaria Patrizia Stoppelli
Aug 14, 2020·Journal of Peptide Science : an Official Publication of the European Peptide Society·Antonio MazzoleniPaolo Rovero

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