Selective chemical protein modification (original) (raw)
Walsh, C. T. Posttranslational Modification of Proteins: Expanding Natures Inventory Roberts and Company Publishers (2006).
de Graaf, A. J., Kooijman, M., Hennink, W. E. & Mastrobattista, E. Nonnatural amino acids for site-specific protein conjugation. Bioconjug. Chem.20, 1281–1295 (2009). ArticleCASPubMed Google Scholar
Chalker, J. M., Bernardes, G. J., Ya, L. & Davis, B. G. Chemical modification of proteins at cysteine: opportunities in chemistry and biology. Chem. Asian J.4, 630–640 (2009). ArticleCASPubMed Google Scholar
Sletten, E. M. & Bertozzi, C. R. Bioorthogonal chemistry: fishing for selectivity in a sea of functionality. Angew. Chem. Int. Ed.48, 6974–6998 (2009). ArticleCAS Google Scholar
Prescher, J. A., Dube, D. H. & Bertozzi, C. R. Chemical remodelling of cell surfaces in living animals. Nature430, 873–877 (2004).The Staudinger ligation was used to undertake chemical modification of cell surfaces in mice for the first time; a powerful early example of in vivo chemistry. ArticleADSCASPubMed Google Scholar
Schnolzer, M. & Kent, S. B. Constructing proteins by dovetailing unprotected synthetic peptides: backbone-engineered HIV protease. Science256, 221–225 (1992). ArticleADSCASPubMed Google Scholar
Zioudrou, C., Wilchek, M. & Patchornik, A. Conversion of the L-serine residue to an L-cysteine residue in peptides. Biochemistry4, 1811–1822 (1965).We consider this paper pivotal in priming the concept of convergent protein synthesis; the ability to selectively ‘chemically mutate’/‘post-expression mutate’ one residue to another has had long standing implications. ArticleCAS Google Scholar
Polgar, L. & Bender, M. L. A new enzyme containing a synthetically formed active site. Thiol-subtilisin. J. Am. Chem. Soc.88, 3153–3154 (1966). ArticleCAS Google Scholar
Neet, K. E. & Koshland, D. E. Jr The conversion of serine at the active site of subtilisin to cysteine: a “chemical mutation”. Proc. Natl Acad. Sci. USA56, 1606–1611 (1966). ArticleADSCASPubMedPubMed Central Google Scholar
Chalker, J. M. & Davis, B. G. Chemical mutagenesis: selective post-expression interconversion of protein amino acid residues. Curr. Opin. Chem. Biol.14, 781–789 (2010). ArticleCASPubMed Google Scholar
Hermanson, G. T. Bioconjugate Techniques 2nd edn Academic Press, Inc. (2008).
Crankshaw, M. W. & Grant, G. A. Modification of Cysteine Wiley (1996).
Clark, P. I. & Lowe, G. Chemical mutations of papain. The preparation of Ser 25- and Gly 25-Papain. J. Chem. Soc. Chem. Commun.24, 923–924 (1977). Article Google Scholar
Goddard, D. R. & Michaelis, L. Derivatives of keratin. J. Biol. Chem.112, 361–371 (1935). CAS Google Scholar
Lundell, N. & Schreitmüller, T. Sample preparation for peptide mapping--A pharmaceutical quality-control perspective. Anal. Biochem.266, 31–47 (1999). ArticleCASPubMed Google Scholar
Stephanopoulos, N., Tong, G. J., Hsiao, S. C. & Francis, M. B. Dual-surface modified virus capsids for targeted delivery of photodynamic agents to cancer cells. ACS Nano4, 6014–6020 (2010). ArticleCASPubMed Google Scholar
Smith, M. E. B. et al. Protein modification, bioconjugation, and disulfide bridging using bromomaleimides. J. Am. Chem. Soc.132, 1960–1965 (2010). ArticleCASPubMedPubMed Central Google Scholar
Betting, D. J., Kafi, K., Abdollahi-fard, A., Hurvitz, S. A. & Timmerman, J. M. Sulfhydryl-based tumor antigen-carrier protein conjugates stimulate superior antitumor immunity against B cell lymphomas. J. Immunol.181, 4131–4140 (2008). ArticleCASPubMed Google Scholar
Zhang, Y., Bhatt, V. S., Sun, G., Wang, P. G. & Palmer, A. F. Site-selective glycosylation of hemoglobin on Cys beta93. Bioconjug. Chem.19, 2221–2230 (2008). ArticleCASPubMedPubMed Central Google Scholar
Shen, B.-Q. et al. Conjugation site modulates the in vivo stability and therapeutic activity of antibody-drug conjugates. Nat. Biotechnol.30, 184–189 (2012). ArticleCASPubMed Google Scholar
Nathani, R. I. et al. Reversible protein affinity-labelling using bromomaleimide-based reagents. Org. Biomol. Chem.11, 2408–2411 (2013). ArticleCASPubMedPubMed Central Google Scholar
Moody, P. et al. Bromomaleimide-linked bioconjugates are cleavable in mammalian cells. Chembiochem13, 39–41 (2012). ArticleADSCASPubMed Google Scholar
Hofer, T., Thomas, J. D., Terrence, R., Burke, J. & Rader, C. An engineered selenocysteine defines a unique class of antibody derivatives. Proc. Natl Acad. Sci. USA105, 12451–12456 (2008). ArticleADSCASPubMedPubMed Central Google Scholar
Kundu, R. & Ball, Z. T. Rhodium-catalyzed cysteine modification with diazo reagents. Chem. Commun.2, 4166–4168 (2012). Google Scholar
Bös, C., Lorenzen, D. & Braun, V. Specific in vivo labeling of cell surface-exposed protein loops: reactive cysteines in the predicted gating loop mark a ferrichrome binding site and a ligand-induced conformational change of the Escherichia coli FhuA protein. J. Bacteriol.180, 605–613 (1998). PubMedPubMed Central Google Scholar
Berglund, P. et al. Chemical modification of cysteine mutants of subtilisin bacillus lentus can create better catalysts than the wild-type enzyme. J. Am. Chem. Soc.119, 5265–5266 (1997).A far-sighted example of using site-selective modification methods to create a logical array of homogenous and precise enzyme variants; here catalytic activity was modulated in a direct manner. ArticleCAS Google Scholar
Davis, B. G., Maughan, M. A. T., Green, M. P., Ullman, A. & Jones, J. B. Glycomethanethiosulfonates: powerful reagents for protein glycosylation. Tetrahedron Asymmetry11, 245–262 (2000). ArticleCAS Google Scholar
Gamblin, D. P. et al. Glycosyl phenylthiosulfonates (glyco-PTS): novel reagents for glycoprotein synthesis. Org. Biomol. Chem.1, 3642–3644 (2003). ArticleCASPubMed Google Scholar
van Kasteren, S. I., Kramer, H. B., Gamblin, D. P. & Davis, B. G. Site-selective glycosylation of proteins: creating synthetic glycoproteins. Nat. Protoc.2, 3185–3194 (2007). ArticleCASPubMed Google Scholar
van Kasteren, S. I. et al. Expanding the diversity of chemical protein modification allows post-translational mimicry. Nature446, 1105–1109 (2007).Two mutually compatible reactions were applied to create different site-selective modifications (S–S and triazole) in di-modified proteins; these acted as effective mimics of natural modifications in vitro and in vivo. ArticleADSCASPubMed Google Scholar
Gamblin, D. P. et al. Glyco-SeS: selenenylsulfide-mediated protein glycoconjugation--a new strategy in post-translational modification. Angew. Chem. Int. Ed.43, 828–833 (2004). ArticleCAS Google Scholar
Gamblin, D. P. et al. Chemical site-selective prenylation of proteins. Mol. Biosyst.4, 558–561 (2008). ArticleCASPubMed Google Scholar
Smith, M. L. et al. Modified tobacco mosaic virus particles as scaffolds for display of protein antigens for vaccine applications. Virology348, 475–488 (2006). ArticleCASPubMed Google Scholar
Kalkhof, S. & Sinz, A. Chances and pitfalls of chemical cross-linking with amine-reactive N-hydroxysuccinimide esters. Anal. Bioanal. Chem.392, 305–312 (2008). ArticleCASPubMed Google Scholar
Nakamura, T., Kawai, Y., Kitamoto, N., Osawa, T. & Kato, Y. Covalent modification of lysine residues by allyl isothiocyanate in physiological conditions: plausible transformation of isothiocyanate from thiol to amine. Chem. Res. Toxicol.22, 536–542 (2009). ArticleCASPubMed Google Scholar
Tanaka, K. et al. A submicrogram-scale protocol for biomolecule-based PET imaging by rapid 6pi-azaelectrocyclization: visualization of sialic acid dependent circulatory residence of glycoproteins. Angew. Chem. Int. Ed.47, 102–105 (2008). ArticleCAS Google Scholar
Jentoft, N. & Dearborn, D. G. Labeling of proteins by reductive methylation using sodium cyanoborohydride. J. Biol. Chem.254, 4359–4365 (1979). CASPubMed Google Scholar
McFarland, J. M. & Francis, M. B. Reductive alkylation of proteins using iridium catalyzed transfer hydrogenation. J. Am. Chem. Soc.127, 13490–13491 (2005). ArticleCASPubMed Google Scholar
Dawson, P. E., Muir, T. W., Clark-Lewis, I. & Kent, S. B. H. Synthesis of proteins by native chemical ligation. Science266, 776–778 (1994).This paper created the benchmark for use of native amide bond formation under protein compatible conditions (native chemical ligation) to join two synthetic peptides to produce full length protein; a prime example of protein synthesis through linear assembly. ArticleADSCASPubMed Google Scholar
Wieland, T., Bokelmann, E., Bauer, L., Lang, H. U. & Lau, H. Uber Peptidsynthesen. 8. Mitteilung Bildung von S-haltingen Peptiden durch intromolekulare Wanderung von Aminoacylresten. Liebigs Ann. Chem.583, 129–149 (1953). ArticleCAS Google Scholar
Dawson, P. E. Native chemical ligation combined with desulfurization and deselenization: a general strategy for chemical protein synthesis. Isr. J. Chem.51, 862–867 (2011). ArticleCAS Google Scholar
Muir, T. W., Sondhi, D. & Cole, P. A. Expressed protein ligation: a general method for protein engineering. Proc. Natl Acad. Sci. USA95, 6705–6710 (1998). ArticleADSCASPubMedPubMed Central Google Scholar
Komarov, A. G., Linn, K. M., Devereaux, J. J. & Valiyaveetil, F. I. Modular strategy for the semisynthesis of a K+ channel: investigating interactions of the pore helix. ACS Chem. Biol.4, 1029–1038 (2009). ArticleCASPubMedPubMed Central Google Scholar
Vila-Perelló, M. et al. Streamlined expressed protein ligation using split inteins. J. Am. Chem. Soc.135, 286–292 (2013). ArticleCASPubMed Google Scholar
Ren, H. et al. A biocompatible condensation reaction for the labeling of terminal cysteine residues on proteins. Angew. Chem. Int. Ed.48, 9658–9662 (2009). ArticleCAS Google Scholar
Staudinger, H. & Meyer, J. Über neue organische Phosphorverbindungen III. Phosphinmethylenderivate und Phosphinimine. Helv. Chim. Acta2, 635–646 (1919). ArticleCAS Google Scholar
Saxon, E. & Bertozzi, C. R. Cell surface engineering by a modified Staudinger reaction. Science287, 2007–2010 (2000). ArticleADSCASPubMed Google Scholar
Kiick, K. L., Saxon, E., Tirrell, D. A. & Bertozzi, C. R. Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc. Natl Acad. Sci. USA99, 19–24 (2002). ArticleADSCASPubMed Google Scholar
Tsao, M.-L., Tian, F. & Schultz, P. G. Selective Staudinger modification of proteins containing p-azidophenylalanine. Chembiochem6, 2147–2149 (2005). ArticleCASPubMed Google Scholar
van Berkel, S. S., van Eldijk, M. B. & van Hest, J. C. M. Staudinger ligation as a method for bioconjugation. Angew. Chem. Int. Ed.50, 8806–8827 (2011). ArticleCAS Google Scholar
Lemieux, G. a., De Graffenried, C. L. & Bertozzi, C. R. A fluorogenic dye activated by the staudinger ligation. J. Am. Chem. Soc.125, 4708–4709 (2003). ArticleCASPubMed Google Scholar
Naganathan, S., Ye, S., Sakmar, T. P. & Huber, T. Site-specific epitope tagging of G protein-coupled receptors by bioorthogonal modification of a genetically encoded unnatural amino acid. Biochemistry52, 1028–1036 (2013). ArticleCASPubMed Google Scholar
Szymański, W., Wu, B., Poloni, C., Janssen, D. B. & Feringa, B. L. Azobenzene photoswitches for Staudinger-Bertozzi ligation. Angew. Chem. Int. Ed.125, 2122–2126 (2013). Article Google Scholar
Nilsson, B. L., Kiessling, L. L. & Raines, R. T. Staudinger ligation: a peptide from a thioester and azide. Org. Lett.2, 1939–1941 (2000). ArticleCASPubMed Google Scholar
Saxon, E., Armstrong, J. I. & Bertozzi, C. R. A. “Traceless” Staudinger ligation for the chemoselective synthesis of amide bonds. Org. Lett.2, 2141–2143 (2000). ArticleCASPubMed Google Scholar
Doores, K. J. et al. Direct deprotected glycosyl-asparagine ligation. Chem. Commun.7, 1401–1403 (2006). ArticleCAS Google Scholar
Bernardes, G. J. L., Linderoth, L., Doores, K. J., Boutureira, O. & Davis, B. G. Site-selective traceless Staudinger ligation for glycoprotein synthesis reveals scope and limitations. Chembiochem12, 1383–1386 (2011). ArticleCASPubMed Google Scholar
Serwa, R. et al. Chemoselective Staudinger-phosphite reaction of azides for the phosphorylation of proteins. Angew. Chem. Int. Ed.48, 8234–8239 (2009). ArticleCAS Google Scholar
Agard, N. J., Baskin, J. M., Prescher, J. A., Lo, A. & Bertozzi, C. R. A comparative study of bioorthogonal reactions with azides. ACS Chem. Biol.1, 644–648 (2006). ArticleCASPubMed Google Scholar
Rostovtsev, V. V., Green, L. G., Fokin, V. V. & Sharpless, K. B. A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew. Chem. Int. Ed.41, 2596–2599 (2002). ArticleCAS Google Scholar
Tornøe, C. W., Christensen, C. & Meldal, M. Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(i)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides. J. Org. Chem.67, 3057–3064 (2002). ArticleCASPubMed Google Scholar
Huisgen, R. 1,3-Dipolar cycloadditions past and future. Angew. Chem. Int. Ed.2, 566–598 (1963). Google Scholar
Dimroth, O. Synthesen mit Diazobenzolimid. Ber. Dtsch. Chem. Ges.36, 909–913 (1903). ArticleCAS Google Scholar
Michael, A. Ueber die Einwirkung von Diazobenzolimid auf Acetylendicarbonsäuremethylester. J. Prakt. Chem.48, 94–95 (1893). Article Google Scholar
Meldal, M. & Tornøe, C. W. Cu-catalyzed azide-alkyne cycloaddition. Chem. Rev.108, 2952–3015 (2008). ArticleCASPubMed Google Scholar
Himo, F. et al. Copper(I)-catalyzed synthesis of azoles. DFT study predicts unprecedented reactivity and intermediates. J. Am. Chem. Soc.127, 210–216 (2005). ArticleCASPubMed Google Scholar
Wang, Q. et al. Bioconjugation by copper(I)-catalyzed azide-alkyne [3+2] cycloaddition. J. Am. Chem. Soc.125, 3192–3193 (2003). ArticleCASPubMed Google Scholar
Speers, A. E., Adam, G. C. & Cravatt, B. F. Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3+2] cycloaddition. J. Am. Chem. Soc.125, 4686–4687 (2003). ArticleCASPubMed Google Scholar
Deiters, A. et al. Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae. J. Am. Chem. Soc.125, 11782–11783 (2003). ArticleCASPubMed Google Scholar
Link, J. & Tirrell, D. Cell surface labeling of Escherichia coli via copper(I)-catalyzed [3+2] cycloaddition. J. Am. Chem. Soc.125, 11164–11165 (2003).CuAAC used for the selective modification of proteins on cell (E. coli) surfaces. ArticleCASPubMed Google Scholar
Link, J., Vink, M. K. S. & Tirrell, D. Presentation and detection of azide functionality in bacterial cell surface proteins. J. Am. Chem. Soc.126, 10598–10602 (2004). ArticleCASPubMed Google Scholar
Dieterich, D. C., Link, J., Graumann, J., Tirrell, D. & Schuman, E. M. Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT). Proc. Natl Acad. Sci. USA103, 9482–9487 (2006). ArticleADSCASPubMedPubMed Central Google Scholar
Link, J. et al. Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids. Proc. Natl Acad. Sci. USA103, 10180–10185 (2006). ArticleADSCASPubMedPubMed Central Google Scholar
Kennedy, D. C. et al. Cellular consequences of copper complexes used to catalyze bioorthogonal click reactions. J. Am. Chem. Soc.133, 17993–18001 (2011). ArticleCASPubMed Google Scholar
Hong, V., Steinmetz, N. F., Manchester, M. & Finn, M. G. Labeling live cells by copper-catalyzed alkyne--azide click chemistry. Bioconjug. Chem.21, 1912–1916 (2010). ArticleCASPubMedPubMed Central Google Scholar
Rae, T. D., Schmidt, P. J., Pufahl, R. A., Culotta, V. C. & V. O'Halloran, T. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science284, 805–808 (1999). ArticleADSCASPubMed Google Scholar
Soriano Del Amo, D. et al. Biocompatible copper(I) catalysts for in vivo imaging of glycans. J. Am. Chem. Soc.132, 16893–16899 (2010). ArticleCASPubMed Google Scholar
Uttamapinant, C. et al. Fast, cell-compatible click chemistry with copper-chelating azides for biomolecular labeling. Angew. Chem. Int. Ed.51, 5852–5856 (2012). ArticleCAS Google Scholar
Deiters, A., Cropp, T. A., Summerer, D., Mukherji, M. & Schultz, P. G. Site-specific PEGylation of proteins containing unnatural amino acids. Bioorg. Med. Chem. Lett.14, 5743–5745 (2004). ArticleCASPubMed Google Scholar
Ribeiro-Viana, R. et al. Virus-like glycodendrinanoparticles displaying quasi-equivalent nested polyvalency upon glycoprotein platforms potently block viral infection. Nat. Commun.3, 1303 (2012). ArticleCASPubMed Google Scholar
Agard, N. J., Prescher, J. a. & Bertozzi, C. R. A strain-promoted [3+2] azide-alkyne cycloaddition for covalent modification of biomolecules in living systems. J. Am. Chem. Soc.126, 15046–15047 (2004). ArticleCASPubMed Google Scholar
Wittig, G. & Krebs, A. Zur Existenz niedergliedriger cycloalkine, I. Chem. Ber.94, 3260–3275 (1961). ArticleCAS Google Scholar
Ning, X., Guo, J., Wolfert, M. A. & Boons, G.-J. Visualizing metabolically labeled glycoconjugates of living cells by copper-free and fast huisgen cycloadditions. Angew. Chem. Int. Ed.47, 2253–2255 (2008). ArticleCAS Google Scholar
Laughlin, S. T., Baskin, J. M., Amacher, S. L. & Bertozzi, C. R. In vivo imaging of membrane-associated glycans in developing zebrafish. Science320, 664–667 (2008). ArticleADSCASPubMedPubMed Central Google Scholar
Jewett, J. C., Sletten, E. M. & Bertozzi, C. R. Rapid Cu-free click chemistry with readily synthesized biarylazacyclooctynones. J. Am. Chem. Soc.132, 3688–3690 (2010). ArticleCASPubMedPubMed Central Google Scholar
Dommerholt, J. et al. Readily accessible bicyclononynes for bioorthogonal labeling and three-dimensional imaging of living cells. Angew. Chem. Int. Ed.49, 9422–9425 (2010). ArticleCAS Google Scholar
Plass, T., Milles, S., Koehler, C., Schultz, C. & Lemke, E. A. Genetically encoded copper-free click chemistry. Angew. Chem. Int. Ed.50, 3878–3881 (2011). ArticleCAS Google Scholar
Lang, K. et al. Genetic encoding of bicyclononynes and trans-cyclooctenes for site-specific protein labeling in vitro and in live mammalian cells via rapid fluorogenic Diels-Alder reactions. J. Am. Chem. Soc.134, 10317–10320 (2012). ArticleCASPubMedPubMed Central Google Scholar
Lo Conte, M. et al. Multi-molecule reaction of serum albumin can occur through thiol-yne coupling. Chem. Commun.47, 11086–11088 (2011). ArticleCAS Google Scholar
Blackman, M. L., Royzen, M. & Fox, J. M. Tetrazine ligation: fast bioconjugation based on inverse-electron-demand Diels-Alder reactivity. J. Am. Chem. Soc.130, 13518–13519 (2008).An early example of inverse electron demand Diels-Alder reactions developed for the modification of proteins; a reaction that appears to be one of the most rapid in protein modification contexts. ArticleCASPubMedPubMed Central Google Scholar
Devaraj, N. K., Weissleder, R. & Hilderbrand, S. Tetrazine-based cycloadditions: application to pretargeted live cell imaging. Bioconjug. Chem.19, 2297–2299 (2008). ArticleCASPubMedPubMed Central Google Scholar
Taylor, M. T., Blackman, M. L., Dmitrenko, O. & Fox, J. M. Design and synthesis of highly reactive dienophiles for the for the tetrazine- trans-cyclooctene ligation. J. Am. Chem. Soc.133, 9646–9649 (2011). ArticleCASPubMedPubMed Central Google Scholar
Seitchik, J. L. et al. Genetically encoded tetrazine amino acid directs rapid site-specific in vivo bioorthogonal ligation with trans-cyclooctenes. J. Am. Chem. Soc.134, 2898–2901 (2012). ArticleCASPubMedPubMed Central Google Scholar
Lang, K. et al. Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction. Nat. Chem.4, 298–304 (2012). ArticleCASPubMedPubMed Central Google Scholar
Plass, T. et al. Amino acids for Diels-Alder reactions in living cells. Angew. Chem. Int. Ed.51, 4166–4170 (2012). ArticleCAS Google Scholar
Kaya, E. et al. A genetically encoded norbornene amino acid for the mild and selective modification of proteins in a copper-free click reaction. Angew. Chem. Int. Ed.51, 4466–4469 (2012). ArticleCAS Google Scholar
Liang, Y., Mackey, J. L., Lopez, S. a., Liu, F. & Houk, K. N. Control and design of mutual orthogonality in bioorthogonal cycloadditions. J. Am. Chem. Soc.134, 17904–17907 (2012). ArticleCASPubMed Google Scholar
Karver, M. R., Weissleder, R. & Hilderbrand, S. A. Bioorthogonal reaction pairs enable simultaneous, selective, multi-target imaging. Angew. Chem. Int. Ed.51, 920–922 (2012). ArticleCAS Google Scholar
Song, W., Wang, Y., Qu, J., Madden, M. M. & Lin, Q. A photoinducible 1,3-dipolar cycloaddition reaction for rapid, selective modification of tetrazole-containing proteins. Angew. Chem. Int. Ed.47, 2832–2835 (2008). ArticleCAS Google Scholar
Song, W., Wang, Y., Qu, J. & Lin, Q. Selective functionalization of a genetically encoded alkene-containing protein via “ photoclick chemistry ” in bacterial cells. J. Am. Chem. Soc.130, 9654–9655 (2008). ArticleCASPubMed Google Scholar
Yu, Z., Pan, Y., Wang, Z., Wang, J. & Lin, Q. Genetically encoded cyclopropene directs rapid, photoclick-chemistry-mediated protein labeling in mammalian cells. Angew. Chem. Int. Ed.51, 10600–10604 (2012). ArticleCAS Google Scholar
Antos, J. M. & Francis, M. B. Transition metal catalyzed methods for site-selective protein modification. Curr. Opin. Chem. Biol.10, 253–262 (2006). ArticleCASPubMed Google Scholar
Dibowski, H. & Schmidtchen, F. P. Bioconjugation of peptides by palladium catalyzed C-C cross-coupling in water. Angew. Chem. Int. Ed.37, 476–478 (1998). ArticleCAS Google Scholar
Ojida, A., Tsutsumi, H., Kasagi, N. & Hamachi, I. Suzuki coupling for protein modification. Tetrahedron Lett.46, 3301–3305 (2005). ArticleCAS Google Scholar
Santoro, S. W., Wang, L., Herberich, B., King, D. S. & Schultz, P. G. An efficient system for the evolution of aminoacyl-tRNA synthetase specificity. Nat. Biotechnol.20, 1044–1048 (2002). ArticleCASPubMed Google Scholar
Kodama, K. et al. Regioselective carbon-carbon bond formation in proteins with palladium catalysis; new protein chemistry by organometallic chemistry. Chembiochem7, 134–139 (2006). ArticleCASPubMed Google Scholar
Kodama, K. et al. Site-specific functionalization of proteins by organopalladium reactions. Chembiochem8, 232–238 (2007). ArticleCASPubMed Google Scholar
Brustad, E. et al. A genetically encoded boronate-containing amino acid. Angew. Chem. Int. Ed.47, 8220–8223 (2008). ArticleCAS Google Scholar
Chalker, J. M., Wood, C. S. C. & Davis, B. G. A convenient catalyst for aqueous and protein Suzuki-Miyaura cross-coupling. J. Am. Chem. Soc.131, 16346–16347 (2009).A highly biocompatible ligand system developed for the efficient modification of proteins by palladium-mediated C–C bond formation, allowing application of one of the most prevalent reactions in Organic Chemistry to Biology. ArticleCASPubMed Google Scholar
Spicer, C. D. & Davis, B. G. Palladium-mediated site-selective Suzuki-Miyaura protein modification at genetically encoded aryl halides. Chem. Commun.47, 1698–1700 (2011). ArticleCAS Google Scholar
Wang, Y.-S. et al. The de novo engineering of pyrrolysyl-tRNA synthetase for genetic incorporation of L-phenylalanine and its derivatives. Mol. Biosyst.7, 714–717 (2011). ArticleCASPubMed Google Scholar
Spicer, C. D., Triemer, T. & Davis, B. G. Palladium-mediated cell-surface labeling. J. Am. Chem. Soc.134, 800–803 (2012). ArticleCASPubMed Google Scholar
Spicer, C. D. & Davis, B. G. Rewriting the bacterial glycocalyx via Suzuki-Miyaura cross-coupling. Chem. Commun.49, 2747–2749 (2013). ArticleCAS Google Scholar
Li, N., Lim, R. K. V., Edwardraja, S. & Lin, Q. Copper-free Sonogashira cross-coupling for functionalization of alkyne-encoded proteins in aqueous medium and in bacterial cells. J. Am. Chem. Soc.133, 15316–15319 (2011). ArticleCASPubMedPubMed Central Google Scholar
Dumas, A. et al. Self-liganded Suzuki-Miyaura coupling for site-selective protein PEGylation. Angew. Chem. Int. Ed.52, 3916–3921 (2013). ArticleCAS Google Scholar
Gao, Z., Gouverneur, V. & Davis, B. G. Enhanced aqueous Suzuki–Miyaura coupling allows site-specific polypeptide 18F-labeling. J. Am. Chem. Soc.135, 13612–13615 (2013). ArticleCASPubMedPubMed Central Google Scholar
Li, J. et al. Ligand-free palladium-mediated site-specific protein labeling inside gram-negative bacterial pathogens. J. Am. Chem. Soc.135, 7330–7338 (2013). ArticleCASPubMed Google Scholar
Lin, Y. A., Chalker, J. M., Floyd, N., Bernardes, G. J. L. & Davis, B. G. Allyl sulfides are privileged substrates in aqueous cross-metathesis: application to site-selective protein modification. J. Am. Chem. Soc.130, 9642–9643 (2008). ArticleCASPubMed Google Scholar
Chalker, J. M., Lin, Y. A., Boutureira, O. & Davis, B. G. Enabling olefin metathesis on proteins: chemical methods for installation of S-allyl cysteine. Chem. Commun. 3714–3716 (2009).
Lin, Y. A., Chalker, J. M. & Davis, B. G. Olefin cross-metathesis on proteins: investigation of allylic chalcogen effects and guiding principles in metathesis partner selection. J. Am. Chem. Soc.132, 16805–16811 (2010). ArticleCASPubMed Google Scholar
Lin, Y. A. et al. Rapid cross metathesis for protein modifications via chemical access to se-allyl selenocysteine in proteins. J. Am. Chem. Soc.135, 12156–12159 (2013). ArticleCASPubMedPubMed Central Google Scholar
Antos, J. M. & Francis, M. B. Selective tryptophan modification with rhodium carbenoids in aqueous solution. J. Am. Chem. Soc.126, 10256–10257 (2004). ArticleCASPubMed Google Scholar
Antos, J. M., McFarland, J. M., Iavarone, A. T. & Francis, M. B. Chemoselective tryptophan labeling with rhodium carbenoids at mild pH. J. Am. Chem. Soc.131, 6301–6308 (2009). ArticleCASPubMedPubMed Central Google Scholar
Popp, B. V. & Ball, Z. T. Structure-selective modification of aromatic side chains with dirhodium metallopeptide catalysts. J. Am. Chem. Soc.132, 6660–6662 (2010). ArticleCASPubMed Google Scholar
Chen, Z. et al. Catalytic protein modification with dirhodium metallopeptides: specificity in designed and natural systems. J. Am. Chem. Soc.134, 10138–10145 (2012). ArticleCASPubMed Google Scholar
Alam, J., Keller, T. H. & Loh, T.-P. Functionalization of peptides and proteins by Mukaiyama aldol reaction. J. Am. Chem. Soc.132, 9546–9548 (2010). ArticleCASPubMed Google Scholar
Han, M.-J., Xiong, D.-C. & Ye, X.-S. Enabling Wittig reaction on site-specific protein modification. Chem. Commun.48, 11079–11081 (2012). ArticleCAS Google Scholar
Wang, L., Zhang, Z., Brock, A. & Schultz, P. G. Addition of the keto functional group to the genetic code of Escherichia coli. Proc. Natl Acad. Sci. USA100, 56–61 (2003). ArticleADSCASPubMed Google Scholar
Dirksen, A. & Dawson, P. E. Rapid oxime and hydrazone ligations with aromatic aldehydes for biomolecular labeling. Bioconjug. Chem.19, 2543–2548 (2008). ArticleCASPubMedPubMed Central Google Scholar
Geoghegan, K. F. & Stroh, J. G. Site-directed conjugation of nonpeptide groups to peptides and proteins via periodate oxidation of a 2-amino alcohol. Application to modification at N-terminal serine. Bioconjug. Chem.3, 138–146 (1992). ArticleCASPubMed Google Scholar
Gilmore, J. M., Scheck, R. A., Esser-Kahn, A. P., Joshi, N. S. & Francis, M. B. N-terminal protein modification through a biomimetic transamination reaction. Angew. Chem. Int. Ed.45, 5307–5311 (2006). ArticleCAS Google Scholar
Scheck, R. A., Dedeo, M. T., Iavarone, A. T. & Francis, M. B. Optimization of a biomimetic transamination reaction. J. Am. Chem. Soc.130, 11762–11770 (2008). ArticleCASPubMed Google Scholar
Scheck, R. A. & Francis, M. B. Regioselective labeling of antibodies through N-terminal transamination. ACS Chem. Biol.2, 247–251 (2007). ArticleCASPubMed Google Scholar
Cornish, V. W., Hahn, K. M. & Schultz, P. G. Site-specific protein modification using a ketone handle. J. Am. Chem. Soc.118, 8150–8151 (1996). ArticleCAS Google Scholar
Zhang, Z. et al. A new strategy for the site-specific modification of proteins in vivo. Biochemistry42, 6735–6746 (2003). ArticleCASPubMed Google Scholar
Huang, Y. et al. Genetic incorporation of an aliphatic keto-containing amino acid into proteins for their site-specific modifications. Bioorg. Med. Chem. Lett.20, 878–880 (2010). ArticleCASPubMed Google Scholar
Zeng, H., Xie, J. & Schultz, P. G. Genetic introduction of a diketone-containing amino acid into proteins. Bioorg. Med. Chem. Lett.16, 5356–5359 (2006). ArticleCASPubMed Google Scholar
Carrico, I. S., Carlson, B. L. & Bertozzi, C. R. Introducing genetically encoded aldehydes into proteins. Nat. Chem. Biol.3, 321–322 (2007). ArticleCASPubMed Google Scholar
Liu, H., Wang, L., Brock, A., Wong, C.-H. & Schultz, P. G. A method for the generation of glycoprotein mimetics. J. Am. Chem. Soc.125, 1702–1703 (2003). ArticleCASPubMed Google Scholar
Ye, S. et al. Site-specific incorporation of keto amino acids into functional G protein-coupled receptors using unnatural amino acid mutagenesis. J. Biol. Chem.283, 1525–1533 (2008). ArticleCASPubMed Google Scholar
Hutchins, B. M. et al. Site-specific coupling and sterically controlled formation of multimeric antibody fab fragments with unnatural amino acids. J. Mol. Biol.406, 595–603 (2011). ArticleCASPubMedPubMed Central Google Scholar
Hudak, J. E. et al. Synthesis of heterobifunctional protein fusions using copper-free click chemistry and the aldehyde tag. Angew. Chem. Int. Ed.51, 4161–4165 (2012). ArticleCAS Google Scholar
Kim, C. H. et al. Synthesis of bispecific antibodies using genetically encoded unnatural amino acids. J. Am. Chem. Soc.134, 9918–9921 (2012). ArticleCASPubMedPubMed Central Google Scholar
Brustad, E. M., Lemke, E., Schultz, P. G. & Deniz, A. A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer. J. Am. Chem. Soc.130, 17664–17665 (2008). ArticleCASPubMedPubMed Central Google Scholar
Sasaki, T., Kodama, K., Suzuki, H., Fukuzawa, S. & Tachibana, K. N-terminal labeling of proteins by the Pictet-Spengler reaction. Bioorg. Med. Chem. Lett.18, 4550–4553 (2008). ArticleCASPubMed Google Scholar
Agarwal, P., Weijden, J. V. D., Sletten, E. M., Rabuka, D. & Bertozzi, C. R. A Pictet-Spengler ligation for protein chemical modification. Proc. Natl Acad. Sci. USA110, 46–51 (2012). ArticleADSPubMedPubMed Central Google Scholar
Wang, J., Schiller, S. M. & Schultz, P. G. A biosynthetic route to dehydroalanine-containing proteins. Angew. Chem. Int. Ed.119, 6973–6975 (2007). Article Google Scholar
Guo, J., Wang, J., Lee, J. S. & Schultz, P. G. Site-specific incorporation of methyl- and acetyl-lysine analogues into recombinant proteins. Angew. Chem. Int. Ed.120, 6499–6501 (2008). Article Google Scholar
Bernardes, G. J. L., Chalker, J. M., Errey, J. C. & Davis, B. G. Facile conversion of cysteine and alkyl cysteines to dehydroalanine on protein surfaces: versatile and switchable access to functionalized proteins. J. Am. Chem. Soc.130, 5052–5053 (2008). ArticleCASPubMed Google Scholar
Chalker, J. M. et al. Methods for converting cysteine to dehydroalanine on peptides and proteins. Chem. Sci.2, 1666–1676 (2011). ArticleCAS Google Scholar
Chalker, J. M., Lercher, L., Rose, N. R., Schofield, C. J. & Davis, B. G. Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications. Angew. Chem. Int. Ed.51, 1835–1839 (2012). ArticleCAS Google Scholar
Wang, Z. U. et al. A facile method to synthesize histones with posttranslational modification mimics. Biochemistry51, 5232–5234 (2012). ArticleCASPubMed Google Scholar
Floyd, N., Vijayakrishnan, B., Koeppe, J. R. & Davis, B. G. Thiyl glycosylation of olefinic proteins: S-linked glycoconjugate synthesis. Angew. Chem. Int. Ed.48, 7798–7802 (2009). ArticleCAS Google Scholar
Chalker, J. M., Bernardes, J. L., Davis, B. G. & Bernardes, G. J. L. A "tag-and-modify" approach to site-selective protein modification. Acc. Chem. Res.44, 730–741 (2011). ArticleCASPubMed Google Scholar
Chen, Y.-X., Triola, G. & Waldmann, H. Bioorthognal chemistry for site-specific labeling and surface immobilization of proteins. Acc. Chem. Res.44, 762–773 (2011). ArticleCASPubMed Google Scholar
Moore, J. E. & Ward, W. H. Cross-linking of bovine plasma albumin and wool keratin. J. Am. Chem. Soc.78, 2414–2418 (1948). Article Google Scholar
Seim, K. L., Obermeyer, A. C. & Francis, M. B. Oxidative modification of native protein residues using cerium(IV) ammonium nitrate. J. Am. Chem. Soc.133, 16970–16976 (2011). ArticleCASPubMedPubMed Central Google Scholar
Schlick, T. L., Ding, Z., Kovacs, E. W. & Francis, M. B. Dual-surface modification of the tobacco mosaic virus. J. Am. Chem. Soc.127, 3718–3723 (2005). ArticleCASPubMed Google Scholar
McFarland, J. M., Joshi, N. S. & Francis, M. B. Characterization of a three-component coupling reaction on proteins by isotopic labeling and nuclear magnetic resonance spectroscopy. J. Am. Chem. Soc.130, 7639–7644 (2008). ArticleCASPubMed Google Scholar
Tilley, S. D. & Francis, M. B. Tyrosine-selective protein alkylation using pi-allylpalladium complexes. J. Am. Chem. Soc.128, 1080–1081 (2006). ArticleCASPubMed Google Scholar
Espuña, G. et al. Iodination of proteins by IPy2BF4, a new tool in protein chemistry. Biochemistry4, 5957–5963 (2006). ArticleCAS Google Scholar
Hooker, J. M., Esser-Kahn, A. P. & Francis, M. B. Modification of aniline containing proteins using an oxidative coupling strategy. J. Am. Chem. Soc.128, 15558–15559 (2006). ArticleCASPubMed Google Scholar
Carrico, Z. M., Romanini, D. W., Mehl, R. & Francis, M. B. Oxidative coupling of peptides to a virus capsid containing unnatural amino acids. Chem. Commun. 1205–1207 (2008).
Tong, G. J., Hsiao, S. C., Carrico, Z. M. & Francis, M. B. Viral capsid DNA aptamer conjugates as multivalent cell-targeting vehicles. J. Am. Chem. Soc.131, 11174–11178 (2009). ArticleCASPubMedPubMed Central Google Scholar
Wittrock, S., Becker, T. & Kunz, H. Synthetic vaccines of tumor-associated glycopeptide antigens by immune-compatible thioether linkage to bovine serum albumin. Angew. Chem. Int. Ed.46, 5226–5230 (2007). ArticleCAS Google Scholar
Li, Y. et al. Genetically encoded alkenyl–pyrrolysine analogues for thiol–ene reaction mediated site-specific protein labeling. Chem. Sci.3, 2766–2766 (2012). ArticleADSCAS Google Scholar
Dondoni, A., Massi, A., Nanni, P. & Roda, A. A new ligation strategy for peptide and protein glycosylation: photoinduced thiol-ene coupling. Chem. Eur. J.15, 11444–11449 (2009). ArticleCASPubMed Google Scholar
Li, Y., Pan, M., Li, Y., Huang, Y. & Guo, Q. Thiol-yne radical reaction mediated site-specific protein labeling via genetic incorporation of an alkynyl-L-lysine analogue. Org. Biomol. Chem.11, 2624–2629 (2013). ArticleCASPubMed Google Scholar
Fleet, G. W. J. & Porter, R. R. Affinity labelling of antibodies with the aryl nitrene as reactive group. Nature224, 511–512 (1969). ArticleADSCAS Google Scholar
Chin, J. W., Martin, A. B., King, D. S., Wang, L. & Schultz, P. G. Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli. Proc. Natl Acad. Sci. USA99, 11020–11024 (2002). ArticleADSCASPubMedPubMed Central Google Scholar
Chin, J. W. et al. Addition of p-azido-L-phenylalanine to the genetic code of Escherichia coli. J. Am. Chem. Soc.124, 9026–9027 (2002). ArticleCASPubMed Google Scholar
Tippmann, E. M., Liu, W., Summerer, D., Mack, A. V. & Schultz, P. G. A genetically encoded diazirine photocrosslinker in Escherichia coli. Chembiochem8, 2210–2214 (2007). ArticleCASPubMed Google Scholar
Chou, C., Uprety, R., Davis, L., Chin, J. W. & Deiters, A. Genetically encoding an aliphatic diazirine for protein photocrosslinking. Chem. Sci.2, 480–480 (2011). ArticleCAS Google Scholar
Griffin, B. A., Adams, S. R. & Tsien, R. Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science281, 269–272 (1998). ArticleADSCASPubMed Google Scholar
Adams, S. R. et al. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J. Am. Chem. Soc.124, 6063–6076 (2002). ArticleCASPubMed Google Scholar
Tsukiji, S., Miyagawa, M., Takaoka, Y., Tamura, T. & Hamachi, I. Ligand-directed tosyl chemistry for protein labeling in vivo. Nat. Chem. Biol.5, 341–343 (2009).A thought-provoking illustration that enhanced inherent or situation-dependent selectivity can be achieved in convergent protein alteration through a range of mechanisms and using even simple reactions. ArticleCASPubMed Google Scholar
Tamura, T., Tsukiji, S. & Hamachi, I. Native FKBP12 engineering by ligand-directed tosyl chemistry: labeling properties and application to photo-cross-linking of protein complexes in vitro and in living cells. J. Am. Chem. Soc.134, 2216–2226 (2012). ArticleCASPubMed Google Scholar
Wang, L., Brock, A., Herberich, B. & Schultz, P. G. Expanding the genetic code of Escherichia coli. Science292, 498–500 (2001).Unnatural amino acids incorporated site-selectively into proteins by amber codon reassignment and suppression has proven to be a lynchpin technique for enabling the creation of substrates for site-selective protein chemistry. ArticleADSCASPubMed Google Scholar
Liu, C. C. & Schultz, P. G. Adding new chemistries to the genetic code. Annu. Rev. Biochem.79, 413–444 (2010). ArticleCASPubMed Google Scholar
Parrish, A. R. et al. Expanding the genetic code of Caenorhabditis elegans using bacterial aminoacyl-tRNA synthetase/tRNA pairs. ACS Chem. Biol.7, 1292–1302 (2012). ArticleCASPubMedPubMed Central Google Scholar