The role of ligand density in the enzymatic glycosylation of carbohydrates presented on self-assembled monolayers of alkanethiolates on gold

Benjamin T. Houseman, Milan Mrksich*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

140 Scopus citations

Abstract

The biological activity of immobilized carbohydrates can show a dramatic dependence on the density of carbohydrate. This is the result of investigations with self-assembled monolayers that present N- acetylglucosamine groups as a model substrate for glycosylation by bovine β- 1,4-galactosyltransferase (GalTase; see picture). Surface plasmon resonance spectroscopy and carbohydrate-binding lectins were used to characterize the reaction at the interface. UDP-Gal = uridine diphosphogalactose.

Original languageEnglish (US)
Pages (from-to)782-785
Number of pages4
JournalAngewandte Chemie - International Edition
Volume38
Issue number6
StatePublished - Mar 15 1999

Keywords

  • Carbohydrates
  • Glycosylations
  • Interfaces monolayers
  • Surface plasmon resonance spectroscopy

ASJC Scopus subject areas

  • Chemistry(all)

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