Coiled coil type neoglycoproteins presenting three lactose residues

Research output: Contribution to journalArticle

Authors

  • Sinclair Sweeney
  • Gemma Bullen
  • Richard Gillis
  • Gary Adams
  • Arthur Rowe
  • Stephen Harding
  • Paul Murphy

Colleges, School and Institutes

Abstract

Scaffold design, synthesis and application is relevant for biomedical research. For example, multivalent interactions, such as those between cell surface glycoproteins and lectins can influence the potency and duration of signalling. The spacing between carbohydrates on their native protein scaffold could be important. Herein, the coiled coil design principle is used to generate synthetic coiled coil type glycoproteins, where three lactose residues are grafted to the coil via N-linkages to asparagine. Molecular modelling indicates that the distance between the galactose anomeric carbon atoms on the neoglycoproteins is ~30 Å. The inclusion of lactose was accommodated in both the final heptad towards the N-terminus, or more centrally in the penultimate heptad. In either case, neither the helicity nor the assembly to the trimeric form was unduly altered by the presence of the disaccharide.

Details

Original languageEnglish
Pages (from-to)1414–1417
JournalTetrahedron Letters
Volume57
Issue number13
Early online date6 Feb 2016
Publication statusPublished - 30 Mar 2016

Keywords

  • Scaffold, Glycosylated, Coiled Coil, Glycocluster