Affinity-based covalent sialyltransferase probes enabled by ligand-directed chemistry.

ABSTRACT: Sialyltransferases (ST) are key enzymes found in, among others, mammals and bacteria that are responsible for producing sialylated glycans, which play critical roles in human health and disease. However, chemical tools to study sialyltransferases have been limited to non-covalent inhibitors and probes that do not allow isolation and profiling of these important enzymes. Here we report a new class of covalent affinity-based probes (AfBP) for ST by using ligand-directed chemistry (LDchem). Our affinity-based probes are armed with a simple to synthesise but robust O-nitrobenzoxadiazole (O-NBD) warhead, which is a lysine-specific S_NAr electrophilic warhead with an advantageous turn-on fluorescence property. We chemoenzymatically synthesised a series of CMP-Neu5Ac based

SUBMITTER: Ong JY 

PROVIDER: S-EPMC11749336 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature