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Cell surface and in vivo interaction of dendrimeric N-glycoclusters

Authors
  • Taichi, Misako1
  • Kitazume, Shinobu2
  • Vong, Kenward1
  • Imamaki, Rie2
  • Kurbangalieva, Almira3
  • Taniguchi, Naoyuki2
  • Tanaka, Katsunori1, 3, 4
  • 1 RIKEN, Biofunctional Synthetic Chemistry Laboratory, 2-1 Hirosawa, Wako-shi, Saitama, 351-0198, Japan , Wako-shi (Japan)
  • 2 RIKEN, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako-shi, Saitama, 351-0198, Japan , Wako-shi (Japan)
  • 3 Kazan Federal University, Biofunctional Chemistry Laboratory, A. Butlerov Institute of Chemistry, 18 Kremlyovskaya street, Kazan, 420008, Russia , Kazan (Russia)
  • 4 JST-PRESTO, 2-1 Hirosawa, Wako-shi, Saitama, 351-0198, Japan , Wako-shi (Japan)
Type
Published Article
Journal
Glycoconjugate Journal
Publisher
Springer-Verlag
Publication Date
May 12, 2015
Volume
32
Issue
7
Pages
497–503
Identifiers
DOI: 10.1007/s10719-015-9594-6
Source
Springer Nature
Keywords
License
Yellow

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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