Unprecedented Affinity Labeling of Carbohydrate-Binding Proteins with s-Triazinyl Glycosides

Bioconjug Chem. 2019 Sep 18;30(9):2332-2339. doi: 10.1021/acs.bioconjchem.9b00432. Epub 2019 Aug 23.

Abstract

Carbohydrate-protein interactions trigger a wide range of biological signaling pathways, the mainstays of physiological and pathological processes. However, there are an incredible number of carbohydrate-binding proteins (CBPs) that remain to be identified and characterized. This study reports for the first time the covalent labeling of CBPs by triazinyl glycosides, a new and promising class of affinity-based glycoprobes. Mono- and bis-clickable triazinyl glycosides were efficiently synthesized from unprotected oligosaccharides (chitinpentaose and 2'-fucosyl-lactose) in a single step. These molecules allow the specific covalent labeling of chitin-oligosaccharide-binding proteins (wheat germ agglutinin WGA and Bc ChiA1 D202A, an inactivated chitinase) and fucosyl-binding lectin (UEA-I), respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Glycosides / chemistry*
  • Receptors, Cell Surface / chemistry*
  • Staining and Labeling
  • Triazines / chemistry*

Substances

  • Glycosides
  • Receptors, Cell Surface
  • Triazines
  • saccharide-binding proteins