On‐Chip Neo‐Glycopeptide Synthesis for Multivalent Glycan Presentation. Mende, M., Tsouka, A., Heidepriem, J., Paris, G., Mattes, D. S., Eickelmann, S., Bordoni, V., Wawrzinek, R., Fuchsberger, F. F., Seeberger, P. H., Rademacher, C., Delbianco, M., Mallagaray, A., & Loeffler, F. F Chemistry – A European Journal, April, 2020.
On‐Chip Neo‐Glycopeptide Synthesis for Multivalent Glycan Presentation [link]Paper  doi  abstract   bibtex   
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. By combining this technique with click chemistry, neo-glycopeptides were produced 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. The two lectins concanavalin A and langerin were probed 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.
@article{mende_chip_2020,
	title = {On‐{Chip} {Neo}‐{Glycopeptide} {Synthesis} for {Multivalent} {Glycan} {Presentation}},
	issn = {0947-6539, 1521-3765},
	url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/chem.202001291},
	doi = {10.1002/chem.202001291},
	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. By combining this technique with click chemistry, neo-glycopeptides were produced 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. The two lectins concanavalin A and langerin were probed 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.},
	language = {en},
	urldate = {2020-05-12},
	journal = {Chemistry – A European Journal},
	author = {Mende, Marco and Tsouka, Alexandra and Heidepriem, Jasmin and Paris, Grigori and Mattes, Daniela S. and Eickelmann, Stephan and Bordoni, Vittorio and Wawrzinek, Robert and Fuchsberger, Felix F. and Seeberger, Peter H. and Rademacher, Christoph and Delbianco, Martina and Mallagaray, Alvaro and Loeffler, Felix F},
	month = apr,
	year = {2020},
	keywords = {Accessories, Application - Microarray Technology, Country - Germany},
	pages = {chem.202001291},
}

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