Recognition of glycans by simple synthetic receptors is a key issue in supramolecular chemistry, endowed with relevant implications in glycobiology and medicine. In this context, glycoproteins featuring N-glycans represent an important biological target, because they are often exploited by enveloped viruses in adhesion and infection processes. However, a direct evidence for their recognition by a synthetic receptor targeting N-glycans is still missing in the literature. Using a combination of glycoengineering and mass spectrometry techniques, we present here the direct evidence of biomimetic recognition of complex-type N-glycans exposed on the receptor-binding domain (RBD) of the wild-type spike protein of SARS-CoV-2 by a biologically active, synthetic receptor.
Biomimetic Recognition of SARS-CoV-2 Receptor-Binding Domain N-Glycans by an Antiviral Synthetic Receptor / C. Santambrogio, M. Toccafondi, L. Donnici, E. Pesce, R. De Francesco, R. Grifantini, E. Ponzini, F. Milanesi, M. Fragai, C. Nativi, S. Roelens, R. Grandori, O. Francesconi. - In: CHEMBIOCHEM. - ISSN 1439-7633. - 26:7(2025), pp. e202500106.1-e202500106.7. [10.1002/cbic.202500106]
Biomimetic Recognition of SARS-CoV-2 Receptor-Binding Domain N-Glycans by an Antiviral Synthetic Receptor
E. Pesce;R. De Francesco;
2025
Abstract
Recognition of glycans by simple synthetic receptors is a key issue in supramolecular chemistry, endowed with relevant implications in glycobiology and medicine. In this context, glycoproteins featuring N-glycans represent an important biological target, because they are often exploited by enveloped viruses in adhesion and infection processes. However, a direct evidence for their recognition by a synthetic receptor targeting N-glycans is still missing in the literature. Using a combination of glycoengineering and mass spectrometry techniques, we present here the direct evidence of biomimetic recognition of complex-type N-glycans exposed on the receptor-binding domain (RBD) of the wild-type spike protein of SARS-CoV-2 by a biologically active, synthetic receptor.| File | Dimensione | Formato | |
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CBIC-26-e202500106.pdf
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