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