Asymmetrically branched precision glycooligomers targeting langerin

Neuhaus, Kira; Wamhoff, Eike-Christian; Freichel, Tanja; Grafmüller, Andrea; Rademacher, Christoph; Hartmann, Laura

doi:10.1021/acs.biomac.9b00906

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Asymmetrically branched precision glycooligomers targeting langerin

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Wamhoff, Eike-Christian
Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Grafmüller, Andrea
Andrea Grafmüller, Theorie & Bio-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;

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引用

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.

引用: https://hdl.handle.net/21.11116/0000-0004-D82E-6

要旨

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.