Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming

Research output: Contribution to journal › Journal article › Research › peer-review

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Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming. / Rogers, J. M.; Suga, H.

In: Organic and Biomolecular Chemistry, Vol. 13, No. 36, 05.08.2015, p. 9353-9363.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rogers, JM & Suga, H 2015, 'Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming', Organic and Biomolecular Chemistry, vol. 13, no. 36, pp. 9353-9363. https://doi.org/10.1039/c5ob01336d

APA

Rogers, J. M., & Suga, H. (2015). Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming. Organic and Biomolecular Chemistry, 13(36), 9353-9363. https://doi.org/10.1039/c5ob01336d

Vancouver

Rogers JM, Suga H. Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming. Organic and Biomolecular Chemistry. 2015 Aug 5;13(36):9353-9363. https://doi.org/10.1039/c5ob01336d

Author

Rogers, J. M. ; Suga, H. / Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming. In: Organic and Biomolecular Chemistry. 2015 ; Vol. 13, No. 36. pp. 9353-9363.

Bibtex

@article{1092a2b43fb84cddba89258614b1c0e0,
title = "Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming",
abstract = "The protein synthesis machinery of the cell, the ribosome and associated factors, is able to accurately follow the canonical genetic code, that which maps RNA sequence to protein sequence, to assemble functional proteins from the twenty or so proteinogenic amino acids. A number of innovative methods have arisen to take advantage of this accurate, and efficient, machinery to direct the assembly of non-proteinogenic amino acids. We review and compare these routes to 'reprogram the genetic code' including in vitro translation, engineered aminoacyl tRNA synthetases, and RNA 'flexizymes'. These studies show that the ribosome is highly tolerant of unnatural amino acids, with hundreds of unusual substrates of varying structure and chemistries being incorporated into protein chains. We also discuss how these methods have been coupled to selection techniques, such as phage display and mRNA display, opening up an exciting new avenue for the production of proteins and peptides with properties and functions beyond that which is possible using proteins composed entirely of the proteinogenic amino acids.",
author = "Rogers, {J. M.} and H. Suga",
year = "2015",
month = aug,
day = "5",
doi = "10.1039/c5ob01336d",
language = "English",
volume = "13",
pages = "9353--9363",
journal = "Organic & Biomolecular Chemistry",
issn = "1470-4358",
publisher = "Royal Society of Chemistry",
number = "36",

}

RIS

TY - JOUR

T1 - Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming

AU - Rogers, J. M.

AU - Suga, H.

PY - 2015/8/5

Y1 - 2015/8/5

N2 - The protein synthesis machinery of the cell, the ribosome and associated factors, is able to accurately follow the canonical genetic code, that which maps RNA sequence to protein sequence, to assemble functional proteins from the twenty or so proteinogenic amino acids. A number of innovative methods have arisen to take advantage of this accurate, and efficient, machinery to direct the assembly of non-proteinogenic amino acids. We review and compare these routes to 'reprogram the genetic code' including in vitro translation, engineered aminoacyl tRNA synthetases, and RNA 'flexizymes'. These studies show that the ribosome is highly tolerant of unnatural amino acids, with hundreds of unusual substrates of varying structure and chemistries being incorporated into protein chains. We also discuss how these methods have been coupled to selection techniques, such as phage display and mRNA display, opening up an exciting new avenue for the production of proteins and peptides with properties and functions beyond that which is possible using proteins composed entirely of the proteinogenic amino acids.

AB - The protein synthesis machinery of the cell, the ribosome and associated factors, is able to accurately follow the canonical genetic code, that which maps RNA sequence to protein sequence, to assemble functional proteins from the twenty or so proteinogenic amino acids. A number of innovative methods have arisen to take advantage of this accurate, and efficient, machinery to direct the assembly of non-proteinogenic amino acids. We review and compare these routes to 'reprogram the genetic code' including in vitro translation, engineered aminoacyl tRNA synthetases, and RNA 'flexizymes'. These studies show that the ribosome is highly tolerant of unnatural amino acids, with hundreds of unusual substrates of varying structure and chemistries being incorporated into protein chains. We also discuss how these methods have been coupled to selection techniques, such as phage display and mRNA display, opening up an exciting new avenue for the production of proteins and peptides with properties and functions beyond that which is possible using proteins composed entirely of the proteinogenic amino acids.

UR - http://www.scopus.com/inward/record.url?scp=84940845423&partnerID=8YFLogxK

U2 - 10.1039/c5ob01336d

DO - 10.1039/c5ob01336d

M3 - Journal article

C2 - 26280393

AN - SCOPUS:84940845423

VL - 13

SP - 9353

EP - 9363

JO - Organic & Biomolecular Chemistry

JF - Organic & Biomolecular Chemistry

SN - 1470-4358

IS - 36

ER -

ID: 244650802