Skip to main content

Research Repository

Advanced Search

Coiled coil type neoglycoproteins presenting three lactose residues

Sweeney, Sinclair M.; Bullen, Gemma A.; Gillis, Richard B.; Adams, Gary G.; Rowe, Arthur J.; Harding, Stephen E.; Tucker, James H.R.; Peacock, Anna F.A.; Murphy, Paul V.


Sinclair M. Sweeney

Gemma A. Bullen

Richard B. Gillis

Gary G. Adams

Arthur J. Rowe

Profile Image

Professor of Applied Biochemistry

James H.R. Tucker

Anna F.A. Peacock

Paul V. Murphy


Scaffold design, synthesis and application are 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.


Sweeney, S. M., Bullen, G. A., Gillis, R. B., Adams, G. G., Rowe, A. J., Harding, S. E., …Murphy, P. V. (2016). Coiled coil type neoglycoproteins presenting three lactose residues. Tetrahedron Letters, 57(13),

Journal Article Type Article
Acceptance Date Feb 1, 2016
Online Publication Date Feb 6, 2016
Publication Date Mar 30, 2016
Deposit Date May 8, 2017
Journal Tetrahedron Letters
Print ISSN 0040-4039
Electronic ISSN 0040-4039
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 57
Issue 13
Keywords Scaffold; Glycosylated; Coiled coil; Glycocluster
Public URL
Publisher URL
Contract Date May 8, 2017