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- W3047288532 abstract "Abstract Binders of langerin could target vaccines to Langerhans cells for improved therapeutic effect. Since langerin has low affinity for monovalent glycan ligands, highly multivalent presentation has previously been key for targeting. Aiming to reduce the amount of ligand required, we rationally designed molecularly defined high‐affinity binders based on the precise display of glycomimetic ligands (Glc2NTs) on DNA‐PNA scaffolds. Rather than mimicking langerin's homotrimeric structure with a C3‐symmetric scaffold, we developed readily accessible, easy‐to‐design bivalent binders. The method considers the requirements for bridging sugar binding sites and statistical rebinding as a means to both strengthen the interactions at single binding sites and amplify the avidity enhancement provided by chelation. This gave a 1150‐fold net improvement over the affinity of the free ligand and provided a nanomolar binder (IC 50 =300 nM) for specific internalization by langerin‐expressing cells." @default.
- W3047288532 created "2020-08-10" @default.
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- W3047288532 date "2020-09-15" @default.
- W3047288532 modified "2023-10-14" @default.
- W3047288532 title "Rational Design of a DNA‐Scaffolded High‐Affinity Binder for Langerin" @default.
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- W3047288532 doi "https://doi.org/10.1002/anie.202006880" @default.
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- W3047288532 hasPublicationYear "2020" @default.
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