Non-canonical amino acid labeling in proteomics and biotechnology

Journal of Biological Engineering
Aya M SalehTamara L Kinzer-Ursem

Abstract

Metabolic labeling of proteins with non-canonical amino acids (ncAAs) provides unique bioorthogonal chemical groups during de novo synthesis by taking advantage of both endogenous and heterologous protein synthesis machineries. Labeled proteins can then be selectively conjugated to fluorophores, affinity reagents, peptides, polymers, nanoparticles or surfaces for a wide variety of downstream applications in proteomics and biotechnology. In this review, we focus on techniques in which proteins are residue- and site-specifically labeled with ncAAs containing bioorthogonal handles. These ncAA-labeled proteins are: readily enriched from cells and tissues for identification via mass spectrometry-based proteomic analysis; selectively purified for downstream biotechnology applications; or labeled with fluorophores for in situ analysis. To facilitate the wider use of these techniques, we provide decision trees to help guide the design of future experiments. It is expected that the use of ncAA labeling will continue to expand into new application areas where spatial and temporal analysis of proteome dynamics and engineering new chemistries and new function into proteins are desired.

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Citations

Nov 14, 2019·Cellular and Molecular Bioengineering·Aya M SalehSarah Calve
Oct 30, 2020·Frontiers in Bioengineering and Biotechnology·Zhenling CuiKirill Alexandrov
Jul 18, 2020·Chembiochem : a European Journal of Chemical Biology·Ella Watkins-DulaneyFrances Arnold
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Feb 18, 2021·ELife·Luca MinatiMassimiliano Clamer
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Apr 5, 2021·Current Opinion in Microbiology·Hao ChenChenguang Fan
Apr 16, 2021·Frontiers in Microbiology·Maria GrimmKatharina Riedel

Methods Mentioned

BETA
aminoacylation
transgenic
biosensor
genetic modification
FRET

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