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submitted on 05.09.2020 and posted on 07.09.2020by Giulio Goti, Cinzia Colombo, Silvia Achilli, Corinne Vivès, michel Thépaut, Franck Fieschi, Anna Bernardi
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.