Single-site glycine-specific labeling of proteins

Landa Purushottam, Srinivasa Rao Adusumalli, Usha Singh, V. B. Unnikrishnan, Dattatraya Gautam Rawale, Mansi Gujrati, Ram Kumar Mishra and Vishal Rai ()
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Landa Purushottam: Indian Institute of Science Education and Research (IISER) Bhopal
Srinivasa Rao Adusumalli: Indian Institute of Science Education and Research (IISER) Bhopal
Usha Singh: Indian Institute of Science Education and Research (IISER) Bhopal
V. B. Unnikrishnan: Indian Institute of Science Education and Research (IISER) Bhopal
Dattatraya Gautam Rawale: Indian Institute of Science Education and Research (IISER) Bhopal
Mansi Gujrati: Indian Institute of Science Education and Research (IISER) Bhopal
Ram Kumar Mishra: Indian Institute of Science Education and Research (IISER) Bhopal
Vishal Rai: Indian Institute of Science Education and Research (IISER) Bhopal

Nature Communications, 2019, vol. 10, issue 1, 1-9

Abstract: 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 fluorophore. A user-friendly protocol delivers analytically pure tagged proteins. The mild reaction conditions do not alter the structure and function of the protein. The cellular uptake of fluorophore-tagged insulin and its ability to activate the insulin-receptor mediated signaling remains unperturbed.

Date: 2019
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DOI: 10.1038/s41467-019-10503-7

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