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  Asymmetrically branched precision glycooligomers targeting langerin

Neuhaus, K., Wamhoff, E.-C., Freichel, T., Grafmüller, A., Rademacher, C., & Hartmann, L. (2019). Asymmetrically branched precision glycooligomers targeting langerin. Biomacromolecules, 20(11), 4088-4095. doi:10.1021/acs.biomac.9b00906.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0004-D82E-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-45D3-F
Genre: Journal Article

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 Creators:
Neuhaus, Kira, Author
Wamhoff, Eike-Christian1, Author              
Freichel, Tanja, Author
Grafmüller, Andrea2, Author              
Rademacher, Christoph1, Author              
Hartmann, Laura, Author
Affiliations:
1Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863300              
2Andrea Grafmüller, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863323              

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Free keywords: Glycomimetic, solid phase synthesis, Langerin, branched scaffold, carbohydrate-protein interactions
 Abstract: Asymmetrically branched precision glycooligomers are synthesized by solid-phase polymer synthesis for studying multivalent carbohydrate-protein interactions. Through the stepwise assembly of Fmoc-protected oligo(amidoamine) building blocks and Fmoc/Dde protected lysine, straightforward variation of structural parameters such as the number and length of arms, as well as the number and position of carbohydrate ligands is achieved. Binding of 1-arm and 3-arm glycooligomers towards lectin receptors Langerin and Concanavalin A (ConA) was evaluated where the smallest 3-arm glycooligomer shows the highest binding towards Langerin and stepwise elongation of one, two or all three arms leads to decreased binding. When directly comparing binding towards Langerin and ConA, we find that structural variation of the scaffold affects glycomimetic ligand binding differently for the different targets, indicating the potential to tune such ligands not only for their avidity but also for their selectivity towards different lectins.

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Language(s): eng - English
 Dates: 2019-10-102019
 Publication Status: Published in print
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 Identifiers: DOI: 10.1021/acs.biomac.9b00906
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Title: Biomacromolecules
  Other : Biomacromolecules
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 20 (11) Sequence Number: - Start / End Page: 4088 - 4095 Identifier: ISSN: 1525-7797