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  On-chip neo-glycopeptide synthesis for multivalent glycan presentation

Mende, M., Tsouka, A., Heidepriem, J., Paris, G., Mattes, D. S., Eickelmann, S., et al. (2020). On-chip neo-glycopeptide synthesis for multivalent glycan presentation. Chemistry – A European Journal. doi:10.1002/chem.202001291.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-4CEB-D Version Permalink: http://hdl.handle.net/21.11116/0000-0006-4CEC-C
Genre: Journal Article

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 Creators:
Mende, Marco1, Author              
Tsouka, Alexandra1, Author              
Heidepriem, Jasmin1, Author              
Paris, Grigori1, Author              
Mattes, Daniela S., Author
Eickelmann, Stephan1, Author              
Bordoni, Vittorio2, Author              
Wawrzinek, Robert3, Author              
Fuchsberger, Felix F.3, Author              
Seeberger, Peter H.4, Author              
Rademacher, Christoph3, Author              
Delbianco, Martina2, Author              
Mallagaray, Alvaro, Author
Löffler, Felix F.1, Author              
Affiliations:
1Felix Löffler, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2385692              
2Martina Delbianco, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2559692              
3Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863300              
4Peter H. Seeberger, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2040285              

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Free keywords: microarrays, laser-induced forward transfer, lectin, click chemistry, combinatorial chemistry
 Abstract: Single glycan-protein interactions are often weak, such that glycan binding partners commonly utilize multiple, spatially defined binding sites to enhance binding avidity and specificity. Current array technologies usually neglect defined multivalent display. Laser-based array synthesis technology allows for flexible and rapid on-surface synthesis of different peptides. Combining this technique with click chemistry, we produced neo-glycopeptides directly on a functionalized glass slide in the microarray format. Density and spatial distribution of carbohydrates can be tuned, resulting in well-defined glycan structures for multivalent display. We probed the two lectins concanavalin A and langerin with different glycans on multivalent scaffolds, revealing strong spacing-, density-, and ligand-dependent binding. In addition, we could also measure the surface dissociation constant. This approach allows for a rapid generation, screening, and optimization of a multitude of multivalent scaffolds for glycan binding.

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Language(s): eng - English
 Dates: 2020-04-21
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1002/chem.202001291
Other: OA angefragt, MS angefragt AP27042020
 Degree: -

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Title: Chemistry – A European Journal
  Other : Chem. – Eur. J.
  Other : Chem. Eur. J.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 0947-6539