Single-site glycine-specific labeling of proteins.

ABSTRACT: Labeling of native proteins invites interest from diverse segments of science. However, there remains the significant unmet challenge in precise labeling at a single site of a protein. Here, we report the site-specific labeling of natural or easy-to-engineer N-terminus Gly in proteins with remarkable efficiency and selectivity. The method generates a latent nucleophile from N-terminus imine that reacts with an aldehyde to deliver an aminoalcohol under physiological conditions. It differentiates N-Gly as a unique target amongst other proteinogenic amino acids. The method allows single-site labeling of proteins in isolated form and extends to lysed cells. It administers an orthogonal aldehyde group primed for late-stage tagging with an affinity tag, ¹⁹F NMR probe, and a fluorophor

SUBMITTER: Purushottam L 

PROVIDER: S-EPMC6557831 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature