Highlights d Dimeric structure of pradimicin (PRM) with mannose binding ability is elucidated d NMR-based calculations provide a reliable binding model of PRM with mannose d Azide-functionalized PRM (PRM-Azide) shows mannose binding specificity in water d PRM-azide fluorescently stains cell wall mannans of Candida rugosa
Pradimicin A (PRM-A) and related
compounds constitute an exceptional
family of natural pigments that show Ca2+-dependent recognition
of d-mannose (Man). Although these compounds hold great promise
as research tools in glycobiology, their practical application has
been severely limited by their inherent tendency to form water-insoluble
aggregates. Here, we demonstrate that the 2-hydroxyethylamide derivative
(PRM-EA) of PRM-A shows little aggregation in neutral aqueous media
and retains binding specificity for Man. We also show that PRM-EA
stains glycoproteins in dot blot assays, whereas PRM-A fails to do
so, owing to severe aggregation. Significantly, PRM-EA is sensitive
to glycoproteins carrying high mannose-type and hybrid-type N-linked
glycans, but not to those carrying complex-type N-linked glycans.
Such staining selectivity has never been observed in conventional
dyes, suggesting that PRM-EA could serve as a unique staining agent
for the selective detection of glycoproteins with terminal Man residues.
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