Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 46, Issue -, Pages 115-122Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2018.07.014
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Funding
- US National Institutes of Health (NIH) [R35GM1122560]
- US National Science Foundation [CHE-1740549]
- Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the Department of Energy [DE-FG02-98ER20311]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R35GM122560] Funding Source: NIH RePORTER
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Synthesis of proteins with non-canonical amino acids via genetic code expansion is at the forefront of synthetic biology. Progress in this field has enabled site-specific incorporation of over 200 chemically and structurally diverse amino acids into proteins in an increasing number of organisms. This has been facilitated by our ability to repurpose aminoacyl-tRNA synthetases to attach non-canonical amino acids to engineered tRNAs. Current efforts in the field focus on overcoming existing limitations to the simultaneous incorporation of multiple non-canonical amino acids or amino acids that differ from the L-alpha-amino acid structure (e.g. D-amino acid or beta-amino acid). Here, we summarize the progress and challenges in developing more selective and efficient aminoacyl-tRNA synthetases for genetic code expansion.
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