{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Santambrogio C"],"funding":["Ministero dell'Università e della Ricerca","Ministero dell'Università e della Ricerca"],"pagination":["e202500106"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12002116"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(7)"],"pubmed_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."],"journal":["Chembiochem : a European journal of chemical biology"],"pubmed_title":["Biomimetic Recognition of SARS-CoV-2 Receptor-Binding Domain N-Glycans by an Antiviral Synthetic Receptor."],"pmcid":["PMC12002116"],"funding_grant_id":["FISR2020IP_01095","PE00000007, INF-ACT"],"pubmed_authors":["Grandori R","Ponzini E","Roelens S","Santambrogio C","Pesce E","Fragai M","Francesconi O","De Francesco R","Toccafondi M","Nativi C","Donnici L","Milanesi F","Grifantini R"],"additional_accession":[]},"is_claimable":false,"name":"Biomimetic Recognition of SARS-CoV-2 Receptor-Binding Domain N-Glycans by an Antiviral Synthetic Receptor.","description":"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.","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2025-07-08T03:11:00.615Z","creation":"2025-07-08T03:11:00.615Z"},"accession":"S-EPMC12002116","cross_references":{"pubmed":["39982661"],"doi":["10.1002/cbic.202500106"]}}