Coiled coil type neoglycoproteins presenting three lactose residues

[Display omitted] 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 nati...

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Bibliographic Details
Published in:Tetrahedron letters 2016-03, Vol.57 (13), p.1414-1417
Main Authors: 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.
Format: Article
Language:English
Subjects:
Carbon
Coiled coil
Coiling
Glycocluster
Glycoprotein
Glycosylated
Helicity
Inclusions
Lactose
Residues
Scaffold
Scaffolds
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Summary:[Display omitted] 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 ∼30Å. 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.
ISSN:0040-4039
1873-3581
DOI:10.1016/j.tetlet.2016.02.005