Platform Synthetic Lectins for Divalent Carbohydrate Recognition in Water

Biomimetic carbohydrate receptors (“synthetic lectins”) have potential as agents for biological research and medicine. However, although effective strategies are available for “all‐equatorial” carbohydrates (glucose, etc.), the recognition of other types of saccharide under natural (aqueous) conditi...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2016-08, Vol.55 (32), p.9311-9315
Main Authors: Carter, Tom S., Mooibroek, Tiddo J., Stewart, Patrick F. N., Crump, Matthew P., Galan, M. Carmen, Davis, Anthony P.
Format: Article
Language:English
Subjects:
Arches
Aromatic compounds
Binding sites
Biological effects
Biological research
Biomimetics
Carbohydrates
Communication
Communications
dendrimers
Fluorescent Dyes - analysis
Lectins
Lectins - chemical synthesis
Lectins - chemistry
Mimicry
Models, Molecular
Molecular Conformation
molecular recognition
Pyrene
Pyrenes - analysis
Receptors
Recognition
supramolecular chemistry
Water - chemistry
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Summary:Biomimetic carbohydrate receptors (“synthetic lectins”) have potential as agents for biological research and medicine. However, although effective strategies are available for “all‐equatorial” carbohydrates (glucose, etc.), the recognition of other types of saccharide under natural (aqueous) conditions is less well developed. Herein we report a new approach based on a pyrene platform with polar arches extending from aryl substituents. The receptors are compatible with axially substituted carbohydrates, and also feature two identical binding sites, thus mimicking the multivalency observed for natural lectins. A variant with negative charges forms 1:2 host/guest complexes with aminosugars, with K1>3000 m−1 for axially substituted mannosamine, whereas a positively charged version binds the important α‐sialyl unit with K1≈1300 m−1. Be my guests: Carbohydrate receptors featuring two equivalent binding sites were designed to target facially amphiphilic substrates. A version with anionic side chains favors aminosugars, whereas a cationic variant binds the biologically important α‐sialyl unit (as shown).
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201603082