A trifunctional probe for generation of fluorogenic glycan-photocrosslinker conjugates.

ABSTRACT: Interactions between cell surface glycans and lectins mediate vital biological processes, yet their characterization is hindered by the low affinity of these binding events. While photoaffinity labeling can capture these interactions, traditional custom probes often demand tedious synthesis, are limited to simple glycans, and lack versatility. To overcome these limitations, we report a trifunctional scaffold enabling modular assembly of glycan probes. This scaffold integrates orthogonal sites for: (i) efficient late-stage ligation of native oligosaccharides via an N-alkoxy-amine, preserving glycan structure; (ii) flexible amide coupling of various photocrosslinkers, including a recently developed fluorogenic azidocoumarin for traceable labeling; and (iii) conjugation to repor

SUBMITTER: Vreulz B 

PROVIDER: S-EPMC12459285 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature