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Double-Modified Glycopolymers from Thiolactones to Modulate Lectin Selectivity and Affinity.

ABSTRACT: Multivalent glycomaterials show high affinity toward lectins but are often nonselective as they lack the precise 3-D presentation found in native glycans. Here, thiolactone chemistry is exploited to enable the synthesis of glycopolymers with both a primary binding (galactose) and a variable secondary binding unit in close proximity to each other on the linker. These polymers are used to target the Cholera toxin B subunit, CTxB, inspired by its native branched glycan target, GM-1. The secondary, nonbinding unit was shown to dramatically modulate affinity and selectivity toward the Cholera toxin. These increasingly complex glycopolymers, assembled using accessible chemistry, can help breach the synthetic/biological divide to obtain future glycomimetics.

SUBMITTER: Wilkins LE

PROVIDER: S-EPMC6326524 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Double-Modified Glycopolymers from Thiolactones to Modulate Lectin Selectivity and Affinity.

Wilkins Laura E LE Badi Nezha N Du Prez Filip F Gibson Matthew I MI

ACS macro letters 20181206 12

Multivalent glycomaterials show high affinity toward lectins but are often nonselective as they lack the precise 3-D presentation found in native glycans. Here, thiolactone chemistry is exploited to enable the synthesis of glycopolymers with both a primary binding (galactose) and a variable secondary binding unit in close proximity to each other on the linker. These polymers are used to target the Cholera toxin B subunit, CTxB, inspired by its native branched glycan target, GM-1. The secondary, ...[more]

PMID: 30662815

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