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Journal Article

On-chip neo-glycopeptide synthesis for multivalent glycan presentation

MPS-Authors
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Mende,  Marco
Felix Löffler, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Tsouka,  Alexandra
Felix Löffler, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons227662

Heidepriem,  Jasmin
Felix Löffler, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Paris,  Grigori
Felix Löffler, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons211052

Eickelmann,  Stephan
Felix Löffler, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Bordoni,  Vittorio
Martina Delbianco, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons202908

Wawrzinek,  Robert
Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Fuchsberger,  Felix F.
Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121849

Seeberger,  Peter H.
Peter H. Seeberger, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Rademacher,  Christoph
Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons187996

Delbianco,  Martina
Martina Delbianco, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons202218

Löffler,  Felix F.
Felix Löffler, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

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, 26(44), 9954-9963. doi:10.1002/chem.202001291.


Cite as: https://hdl.handle.net/21.11116/0000-0006-4CEB-D
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.