Sugar-lectin interactions investigated through affinity capillary electrophoresis

Mingfang Hong, Aaron Cassely, Yehia Mechref, Milos V. Novotny

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


The affinity interactions of Concanavalin A (Con A) with various saccharide oligomers (dextrins, dextrans, and selected N-linked glycans from various glycoproteins) have been investigated through a capillary electrophoresis approach. Con A has shown a notable binding discrimination between the α-1,6-linked dextran and α-1,4-linked dextrin oligomers. Both the binding capacity and binding discrimination appear to decrease with an increase in sugar chainlength. While the core structure of N-linked glycans is deemed to be responsible for the overall binding of various glycans to Con A, the presence of mannose units at the non-reducing ends was found to be very beneficial to the affinity interaction with Con A. Finally, a connection between the glycan-lectin interaction and glycoprotein-lectin interaction has also been suggested.

Original languageEnglish
Pages (from-to)207-216
Number of pages10
JournalJournal of Chromatography B: Biomedical Sciences and Applications
Issue number2
StatePublished - Mar 10 2001


  • Lectins
  • Sugars


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