Abstract
While many examples have been reported that glycoclusters interact with target lectins more strongly than single molecules of glycans, through multivalency effects, literature examples to support lectin interactions/modulations on cell surface and in live animals is quite rare. Our N-glycoclusters, which were efficiently prepared by immobilizing 16 molecules of the asparagine-linked glycans (N-glycans) onto a lysine-based dendron template through histidine-mediated Huisgen cycloaddition, were shown to efficiently detect platelet endothelial cell adhesion molecule (PECAM) on human umbilical vein endothelial cells (HUVEC) as a α(2-6)-sialylated oligosaccharides recognizing lectin. Furthermore, the identity of the N-glycans on our N-glycoclusters allowed control over organ-selective accumulation and serum clearance properties when intravenously injected into mice.
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Acknowledgments
This work was supported in part by Grants-in-Aid for Scientific Research from the Japan Society for the Promotion of Science, No. 23681047, 25560410, 26560438, and 26870859; by a Research Grant from the Mizutani Foundation for Glycoscience; and by a MEXT Grant-in-Aid for Scientific Research (C) (No. 25430122) and on Innovative Areas “Chemical Biology of Natural Products: Target ID and Regulation of Bioactivity” (No. 26102743). This work was also performed under the Russian Government Program of Competitive Growth of Kazan Federal University.
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Taichi, M., Kitazume, S., Vong, K. et al. Cell surface and in vivo interaction of dendrimeric N-glycoclusters. Glycoconj J 32, 497–503 (2015). https://doi.org/10.1007/s10719-015-9594-6
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DOI: https://doi.org/10.1007/s10719-015-9594-6