Journal
CHEMICAL SCIENCE
Volume 11, Issue 47, Pages -Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0sc03741a
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Funding
- ANR/DFG French-German GLYCOMIME project [ANR-AAPG-2017]
- Glyco@Alps [ANR-15-IDEX02]
- Labex Arcane/CBH-EUR-GS [ANR-17-EURE-0003]
- Synchrotron SOLEIL
- MiUR (Prin 2015)
- European Union's framework program for Research and Innovation Horizon 2020 (2014-2020) under the Marie-Slodowska Curie Grant [675555]
- Regione Toscana (CERM-TT)
- Regione Toscana (BioEnable)
- Recombinant Proteins JOYNLAB, MIUR Italy [PRIN 2017A2KEPL]
- Progetto finanziato dalla Cassa di Risparmio di Firenze 2017 Sviluppo di strategie innovative per la caratterizzazione a dettaglio atomico di coniugati proteina-polimeri per uso terapeutico (Bouncy NMR)
- MiUR
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Two orthogonal, metal free click reactions, enabled to glycosylate ubiquitin and its mutant A28C forming two protein scaffolds with high affinity for BambL, a lectin from the human pathogen Burkholderia ambifaria. A new fucoside analogue, with high affinity with BambL, firstly synthetized and co-crystallized with the protein target, provided the insights for sugar determinants grafting onto ubiquitin. Three ubiquitin-based glycosides were thus assembled. Fuc-Ub, presented several copies of the fucoside analogue, with proper geometry for multivalent effect; Rha-A28C, displayed one thio-rhamnose, known for its ability to tuning the immunological response; finally, Fuc-Rha-A28C, included both multiple fucoside analogs and the rhamnose residue. Fuc-Ub and Fuc-Rha-A28C ligands proved high affinity for BambL and unprecedented immune modulatory properties towards macrophages activation.
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