Experimental investigation examines affinities of mannosyl triazoles in galectin interactions, suggesting new avenues for inhibition.
Mannosyl β-C-1 amidotriazoles have previously been reported to have higher selectivity for galectin-9N (N-terminal domain) than the corresponding galactoside C3 amidotriazoles have, which were more selective for galectin-3. This study further investigated this by synthesis of mono- and bis-aryltriazolyl mannoside analogues to known high-affinity galectin-3 galactosyl-derived inhibitors. Following synthesis, affinity measurements using competititve fluorescence polarization assays were performed which indicated low affinity of the bis-aryltriazolyl mannosyls, while the mono-aryltriazolyl mannosyls analogs possessed improved affinity, albeit with lower and selectivity. From conformational calculations it was implied that the weak-binding bis-aryltriazolyl mannosyl analogues do not find the same conformation and binding pose as the parent galactoside compounds.
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Sjövall et al. (2026) studied this question.
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