ArticleMethods in molecular biology (Clifton, N.J.)2026
Protein Modification via Bioorthogonal HS-BCN Ligation.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Bioorthogonal reactions offer a powerful tool for site-specific labeling of biomolecules in living systems. Among them, the recently reported hydrazonyl sultone (HS)-bicyclo[6.1.0]non-4-yne (BCN) ligation reaction stands out for its fast reaction kinetics and tunable aqueous stability. Herein, we describe the experimental protocols of using HS-BCN ligation for site-specific modification of a recombinant nanobody in vitro and a G protein-coupled receptor (GPCR) on a live mammalian cell surface. These protocols include the genetic encoding of BCN-lysine (BCNK) into the target protein, bioorthogonal modification of the BCNK-encoded proteins, and characterization of the reaction rate and selectivity. Together with the robust genetic encoding of the strained alkyne BCN in any protein structure, the HS-BCN ligation reaction promises to expand the capabilities of bioorthogonal chemistry to enable facile modifications of domain antibodies in vitro for diagnostic applications and selective fluorescent labeling of GPCRs for biophysical studies of receptor dynamics in live cells.
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