Structure-Based Design of Glycodendrimer Antagonists for Improved DC-SIGN Targeting

07 September 2020, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

DC-SIGN multivalent antagonists have emerged as effective antiadhesive agents against various pathogen infections. Recently, our group have shown that high potency can be achieved upon bridging two of the four binding sites displayed by the protein. Here we present our endeavors to accomplish the tetracoordination of DC-SIGN through the synthesis of two cross-shaped glycodendrimers. The choice of a tailored rigid scaffold allowed multivalent presentation of glycomimetics in a spatially defined fashion, while providing good water solubility to the constructs. Evaluation of the biological activity by SPR assay revealed strong binding avidity towards DC-SIGN and increased selectivity over langerin.

Keywords

Glycodendrimers Multivalent glycoconjugates
Glycomimetic Ligands
DC-SIGN interactions
Langerin
surface plasmon resonance

Supplementary materials

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