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  Automated glycan assembly of 19F labelled glycan probes enables high‐throughput NMR studies of protein‐glycan interactions

Fittolani, G., Shanina, E., Guberman, M., Seeberger, P. H., Rademacher, C., & Delbianco, M. (2021). Automated glycan assembly of 19F labelled glycan probes enables high‐throughput NMR studies of protein‐glycan interactions. Angewandte Chemie International Edition, 60(24), 13302-13309. doi:10.1002/anie.202102690.

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 Creators:
Fittolani, Giulio1, Author              
Shanina, Elena2, Author              
Guberman, Mónica3, Author              
Seeberger, Peter H.4, Author              
Rademacher, Christoph2, Author              
Delbianco, Martina1, Author              
Affiliations:
1Martina Delbianco, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2559692              
2Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863300              
3Peter H. Seeberger - Vaccine Development, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863308              
4Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863306              

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Free keywords: glycans, automated glycan assembly, 19F NMR, lectins, protein-glycan interactions
 Abstract: Protein‐glycan interactions mediate important biological processes, including pathogen host invasion and cellular communication. Major challenges to monitoring these low affinity interactions are the required high sensitivity of a biophysical assay and to cover a breath of synthetic well‐defined structures. Here, we showcase an expedite approach that integrates automated glycan assembly (AGA) of 19 F labelled probes and high‐throughput NMR methods, enabling the study of protein‐glycan interactions. Synthetic Lewis type 2 antigens were screened against seven glycan binding proteins (GBPs), including DC‐SIGN and BambL, respectively involved in HIV‐1 and lung infections in immunocompromised patients, confirming the preference for fucosylated glycans (Le x , H type 2, Le y ). Previously unknown glycan‐lectin weak interactions were detected, and thermodynamic data were obtained. Enzymatic reactions were monitored in real‐time, delivering kinetic parameters. These results demonstrate the utility of AGA combined with 19 F NMR for the discovery and characterization of glycan‐protein interactions, opening up new perspectives for 19 F labelled complex glycans.

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Language(s): eng - English
 Dates: 2021-03-302021
 Publication Status: Published in print
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 Rev. Type: Peer
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Title: Angewandte Chemie International Edition
  Abbreviation : Angew. Chem., Int. Ed.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 60 (24) Sequence Number: - Start / End Page: 13302 - 13309 Identifier: ISSN: 1433-7851

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Title: Angewandte Chemie
  Abbreviation : Angew. Chem.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 133 (24) Sequence Number: - Start / End Page: 13414 - 13421 Identifier: ISSN: 0044-8249