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Non‐Canonical Amino Acids in Protein Polymer Design

Connor, Rebecca E., Tirrell, David A.·2007·Polymer Reviews

DOI 10.1080/15583720601109552

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Abstract

Protein polymers can be prepared with essentially absolute control of chain length, sequence, and stereochemistry through biological synthesis in microbial hosts. But for the polymer chemist, the twenty “canonical” amino acids provide an unacceptably small set of starting materials for macromolecular design. In the past several years, powerful techniques have been developed to introduce non‐natural (non‐canonical) amino acids containing a wide variety of functional groups into recombinant proteins. This review presents the methods currently available for the introduction of non‐natural amino acids into engineered proteins both in vitro and in vivo. Methods for multiple‐ and single‐site introduction are described. Recent applications of these methods are also addressed, particularly the development of biosensors, novel surfaces, and materials.

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A Strain-Promoted [3 + 2] Azide−Alkyne Cycloaddition for Covalent Modification of Biomolecules in Living Systems
Agard, N. J., Prescher, J. A., & Bertozzi, C. R. (2004) · Journal of the American Chemical Society · doi:10.1021/ja044996f · Cited by 3,160
Cell Surface Engineering by a Modified Staudinger Reaction
Saxon, E., & Bertozzi, C. R. (2000) · Science · doi:10.1126/science.287.5460.2007 · Cited by 2,463
Expanding the Genetic Code of Escherichia coli
Wang, L., Brock, A., Herberich, B., & Schultz, P. G. (2001) · Science · doi:10.1126/science.1060077 · Cited by 1,504
A General Method for Site-specific Incorporation of Unnatural Amino Acids into Proteins
Noren, C. J., Anthony-Cahill, S. J., Griffith, M. C., & Schultz, P. G. (1989) · Science · doi:10.1126/science.2649980 · Cited by 1,019
Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three‐dimensional structure.
Hendrickson, W. A., Horton, J. R., & LeMaster, D. M. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08287.x · Cited by 1,015
Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
Kiick, K. L., Saxon, E., Tirrell, D. A., & Bertozzi, C. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012583299 · Cited by 911
Self-citation
Expanding the Genetic Code
Wang, L., & Schultz, P. G. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200460627 · Cited by 661
Cell Surface Labeling of Escherichia coli via Copper(I)-Catalyzed [3+2] Cycloaddition
Link, A. J., & Tirrell, D. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja036765z · Cited by 578
Self-citation
Code for collagen's stability deciphered
Holmgren, S. K., Taylor, K. M., Bretscher, L. E., & Raines, R. T. (1998) · Nature · doi:10.1038/33573 · Cited by 499
Modern Separation Techniques for the Efficient Workup in Organic Synthesis
Tzschucke, C. C., Märkert, C., Bannwarth, W., Roller, S., Hebel, A., & Haag, R. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20021104)41:21 · Cited by 354

Show all 92 references

Research works printed but not linked: 1

Pratt E. A., 1974, Fed. Proc., 33, 1463

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Authors: Connor, R. E., & Tirrell, D. A.
Affiliations: California Institute of Technology (US)
Corresponding author: Tirrell, David A.
ORCID: Connor, Rebecca E.
Tirrell, David A.
Venue: Polymer Reviews
Publisher: Informa UK Limited
Published: 2007-04
Volume: 47
Issue: 1
Pages: 9-28
ISSN: 0736-6574 (ISSN-L)
1558-3724
1558-3716
DOI: 10.1080/15583720601109552
OpenAlex: W1981527166
Cited by: 103
References: 92
Citations by year: 2025: 3 · 2024: 3 · 2023: 3 · 2022: 6 · 2021: 3 · 2020: 3 · 2019: 5 · 2018: 1 · 2017: 4 · 2016: 4 · 2015: 2 · 2014: 5 · 2013: 10 · 2012: 9
FWCI: 3.95
Type: journal article
Language: en
Open access: closed
Locations: Journal of macromolecular science. Part C, Reviews in macromolecular chemistry and physics/Journal of macromolecular science. Reviews in macromolecular chemistry and physics (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
Keywords: unnatural amino acids, protein polymers, engineered proteins, biosensors, biomaterials

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Non‐Canonical Amino Acids in Protein Polymer Design

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