конъюгаты с фс

(213)Thygesen, M. B., Sorensen, K. K., Clo, E., and Jensen, K. J. (2009) Direct chemoselective synthesis of glyconanoparticles from

unprotected reducing glycans and glycopeptide aldehydes. Chem. Commun. 6367–6369.

(214)Thygesen, M. B., Sauer, J., and Jensen, K. J. (2009) Chemoselective capture of glycans for analysis on gold nanoparticles: carbohy-

drate oxime tautomers provide functional recognition by proteins.

Chem.—Eur. J. 15, 1649–1660.

(215)Liu, Y., Feizi, T., Carnpanero-Rhodes, M. A., Childs, R. A., Zhang, Y., Mulloy, B., Evans, P. G., Osborn, H. M. I., Otto, D., Crocker, P. R., and Chai, W. (2007) Neoglycolipid probes prepared via oxime ligation for microarray analysis of oligosaccharide-protein interactions.

Chem. Biol. 14, 847–859.

(216)Kovacs, E. W., Hooker, J. M., Romanini, D. W., Holder, P. G., Berry, K. E., and Francis, M. B. (2007) Dual-surface-modified bacteriophage MS2 as an ideal sca old for a viral capsid-based drug delivery system. Bioconjugate Chem. 18, 1140–1147.

(217)Dawson, P. E., and Kent, S. B. H. (2000) Synthesis of native proteins by chemical ligation. Annu. Rev. Biochem. 69, 923–960.

(218)Dawson, P. E., Muir, T. W., Clark-Lewis, I., and Kent, S. B.

(1994) Synthesis of proteins by native chemical ligation. Science

226, 776–779.

(219)Dawson, P. E., Churchill, M. J., Ghadiri, M. R., and Kent, S. B. H. (1997) Modulation of reactivity in native chemical ligation through the use of thiol additives. J. Am. Chem. Soc. 119, 4325–4329.

(220)Reulen, S. W. A., Baal, I. v., Raats, J. M. H., and Merkx, M. (2009) E cient, chemoselective synthesis of immunomicelles using single-domain antibodies with a C-terminal thioester. BMC Biotechnol. 9, 66.

(221)Reulen, S. W. A., Dankers, P. Y. W., Bomans, P. H. H., Meijer, E. W., and Merkx, M. (2009) Collagen targeting using protein-functio-

nalized micelles: the strength of multiple weak interactions. J. Am. Chem. Soc. 131, 7304–7312.

(222)Reulen, S. W. A., Brusselaars, W. W. T., Langereis, S., Mulder, W. J. M., Breurken, M., and Merkx, M. (2007) Protein-Liposome

conjugates using cysteine-lipids and native chemical ligation. Bioconjugate Chem. 18, 590–596.

(223)Yu, C. C., Lin, P. C., and Lin, C. C. (2008) Site-specific immobilization of CMP-sialic acid synthetase on magnetic nanoparticles

and its use in the synthesis of CMP-sialic acid. Chem. Commun. 1308–1310.

(224)Becker, C. F. W., Marsac, Y., Hazarika, P., Moser, J., Goody, R. S., and Niemeyer, C. M. (2007) Functional immobilization of small GTPase Rab6A on DNA-gold nanoparticles by using a site-specifically attached poly(ethylene gylcol) linker and thiol place-exchange reaction.

ChemBioChem 8, 32–36.

(225)Evans, T. C., and Xu, M. Q. (2002) Mechanistic and kinetic considerations of protein splicing. Chem. Rev. 102, 4869–4883.

(226)Muir, T. W. (2003) Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 72, 249–289.

(227)Perler, F. B., and Adam, E. (2000) Protein splicing and its applications. Curr. Opin. Biotechnol. 11, 377–383.

(228)Miller, L. W., and Cornish, V. W. (2005) Selective chemical labeling of proteins in living cells. Curr. Opin. Chem. Biol. 9, 56–61.

(229)Gogarten, J. P., Senejani, A. G., Zhaxybayeva, O., Olendzenski, L., and Hilario, E. (2002) Inteins: Structure, function, and evolution.

Annu. Rev. Microbiol. 56, 263–287.

(230)Camarero, J. A. (2008) Recent developments in the sitespecific immobilization of proteins onto solid supports. Biopolymers 90, 450–458.

(231)Xia, Z. Y., Xing, Y., So, M. K., Koh, A. L., Sinclair, R., and Rao, J. H. (2008) Multiplex detection of protease activity with quantum dot nanosensors prepared by intein-mediated specific bioconjugation. Anal. Chem. 80, 8649–8655.

(232)Chu, N. K., Olschewski, D., Seidel, R., Winklhofer, K. F., Tatzelt, J., Engelhard, M., and Becker, C. F. W. (2010) Protein immobilization on liposomes and lipid-coated nanoparticles by protein trans-splicing. J. Pept. Sci. 16, 582–588.

(233)Datta, A., Hooker, J. M., Botta, M., Francis, M. B., Aime, S., and Raymond, K. N. (2008) High relaxivity gadolinium hydroxypyr-

idonate-viral capsid conjugates: Nanosized MRI contrast agents. J. Am. Chem. Soc. 130, 2546–2552.

(234)Hooker, J. M., O’Neil, J. P., Romanini, D. W., Taylor, S. E., and

Francis, M. B. (2008) Genome-free viral capsids as carriers for positron emission tomography radiolabels. Mol. Imaging Biol. 10, 182–191.

(235)Kovacs, E. W., Hooker, J. M., Romanini, D. W., Holder, P. G., Berry, K. E., and Francis, M. B. (2007) Dual-surface-modified bacteriophage MS2 as an ideal sca old for a viral capsid-based drug delivery system. Bioconjugate Chem. 18, 1140–1147.

(236)Hooker, J. M., Datta, A., Botta, M., Raymond, K. N., and Francis, M. B. (2007) Magnetic resonance contrast agents from viral

capsid shells: A comparison of exterior and interior cargo strategies.

Nano Lett. 7, 2207–2210.

(237)Schlick, T. L., Ding, Z., Kovacs, E. W., and Francis, M. B. (2005) Dual-surface modification of the tobacco mosaic virus. J. Am. Chem. Soc. 127, 3718–3723.

(238)Bruckman, M. A., Kaur, G., Lee, L. A., Xie, F., Sepulveda, J., Breitenkamp, R., Zhang, X., Joralemon, M., Russell, T. P., Emrick, T., and Wang, Q. (2008) Surface modification of tobacco mosaic virus with “click” chemistry. ChemBioChem 9, 519–523.

(239)Carrico, Z. M., Romanini, D. W., Mehl, R. A., and Francis, M. B. (2008) Oxidative coupling of peptides to a virus capsid containing unnatural amino acids. Chem. Commun. 1205–1207.

(240)Stephanopoulos, N., Carrico, Z. M., and Francis, M. B. (2009) Nanoscale integration of sensitizing chromophores and porphyrins with bacteriophage MS2. Angew. Chem., Int. Ed. 48, 9498–9502.

(241)Tong, G. J., Hsiao, S. C., Carrico, Z. M., and Francis, M. B. (2009) Viral capsid DNA aptamer conjugates as multivalent celltargeting vehicles. J. Am. Chem. Soc. 131, 11174–11178.

(242)Irrgang, J., Ksienczyk, J., Lapiene, V., and Niemeyer, C. M. (2009) Analysis of non-covalent bioconjugation of colloidal nanoparticles by means of atomic force microscopy and data clustering. ChemPhysChem 10, 1483–1491.

(243)Delehanty, J. B., Medintz, I. L., Pons, T., Brunel, F. M., Dawson, P. E., and Mattoussi, H. (2006) Self-assembled quantum dotpeptide bioconjugates for selective intracellular delivery. Bioconjugate Chem. 17, 920–927.

(244)Sapsford, K. E., Pons, T., Medintz, I. L., Higashiya, S., Brunel, F. M., Dawson, P. E., and Mattoussi, H. (2007) Kinetics of metal-a nity driven self-assembly between proteins or peptides and CdSe-ZnS quantum dots. J. Phys. Chem. C 111, 11528–11538.

(245)Pons, T., Medintz, I. L., Wang, X., English, D. S., and Mattoussi, H. (2006) Solution-phase single quantum dot fluorescence resonance energy transfer. J. Am. Chem. Soc. 128, 15324–15331.

(246)Medintz, I. L., Konnert, J. H., Clapp, A. R., Stanish, I., Twigg, M. E., Mattoussi, H., Mauro, J. M., and Deschamps, J. R. (2004) A fluorescence resonance energy transfer-derived structure of a quantum dot-protein bioconjugate nanoassembly. Proc. Natl. Acad. Sci. U.S.A. 101, 9612–9617.

(247)Medintz, I. L., Sapsford, K. E., Clapp, A. R., Pons, T., Higashiya, S., Welch, J. T., and Mattoussi, H. (2006) Designer variable repeat length polypeptides as sca olds for surface immobilization of quantum dots. J. Phys. Chem. B 110, 10683–10690.

(248)Pons, T., Medintz, I. L., Sapsford, K. E., Higashiya, S., Grimes, A. F., English, D. S., and Mattoussi, H. (2007) On the quenching of

semiconductor quantum dot photoluminescence by proximal gold nanoparticles. Nano Lett. 7, 3157–3164.

(249)Medintz, I. L., Berti, L., Pons, T., Grimes, A. F., English, D. S., Alessandrini, A., Facci, P., and Mattoussi, H. (2007) A reactive peptidic linker for self-assembling hybrid quantum dot-DNA bioconjugates.

Nano Lett. 7, 1741–1748.

(250)Berti, L., D’Agostino, P. S., Boeneman, K., and Medintz, I. L. (2009) Improved peptidyl linkers for self-assembly of semiconductor quantum dot bioconjugates. Nano Res. 2, 121–129.

(251)Medintz, I. L., Pons, T., Delehanty, J. B., Susumu, K., Brunel, F. M., Dawson, P. E., and Mattoussi, H. (2008) Intracellular delivery of

quantum dot-protein cargos mediated by cell penetrating peptides.

Bioconjugate Chem. 19, 1785–1795.

(252)Clapp, A. R., Medintz, I. L., Mauro, J. M., Fisher, B. R., Bawendi, M. G., and Mattoussi, H. (2003) Fluorescence resonance energy transfer between quantum dot donors and dye-labeled protein acceptors. J. Am. Chem. Soc. 126, 301–310.

(253)Medintz, I. L., Clapp, A. R., Melinger, J. S., Deschamps, J. R., and Mattoussi, H. (2005) A reagentless biosensing assembly based on quantum dot-donor F€orster resonance energy transfer. Adv. Mater. 17, 2450–2455.

(254)Goldman, E. R., Medintz, I. L., Whitley, J. L., Hayhurst, A., Clapp, A. R., Uyeda, H. T., Deschamps, J. R., Lassman, M. E., and Mattoussi, H. (2005) A hybrid quantum dot-antibody fragment fluor-

escence resonance energy transfer-based TNT sensor. J. Am. Chem. Soc. 127, 6744–6751.

(255)Boeneman, K., Mei, B. C., Dennis, A. M., Bao, G., Deschamps, J. R., Mattoussi, H., and Medintz, I. L. (2009) Sensing caspase 3 activity with quantum dot-fluorescent protein assemblies. J. Am. Chem. Soc. 131, 3828–3829.

(256)Medintz, I. L., Clapp, A. R., Mattoussi, H., Goldman, E. R.,

Fisher, B., and Mauro, J. M. (2003) Self-assembled nanoscale biosensors based on quantum dot FRET donors. Nat. Mater. 2, 630–638.

(257)Medintz, I. L., Sapsford, K. E., Clapp, A. R., Pons, T., Higashiya, S., Welch, J. T., and Mattoussi, H. (2006) Designer variable repeat length polypeptides as sca olds for surface immobilization of quantum dots. J. Phys. Chem. B 110, 10683–10690.

(258)Sapsford, K. E., Medintz, I. L., Golden, J. P., Deschamps, J. R., Uyeda, H. T., and Mattoussi, H. (2004) Surface-immobilized self-

assembled protein-based quantum dot nanoassemblies. Langmuir 20, 7720–7728.

(259)Ipe, B. I., and Niemeyer, C. M. (2006) Nanohybrids com-

posed of quantum dots and cytochrome P450 as photocatalysts. Angew. Chem., Int. Ed. 45, 504–507.

(260)Lee, I. S., Lee, N., Park, J., Kim, B. H., Yi, Y. W., Kim, T., Kim, T. K., Lee, I. H., Paik, S. R., and Hyeon, T. (2006) Ni/NiO core/shell

nanoparticles for selective binding and magnetic separation of histidinetagged proteins. J. Am. Chem. Soc. 128, 10658–10659.

(261)Kogot, J. M., England, H. J., Strouse, G. F., and Logan, T. M. (2008) Single peptide assembly onto a 1.5 nm Au surface via a histidine tag. J. Am. Chem. Soc. 130, 16156–16157.

(262)Kogot, J. M., Parker, A. M., Lee, J., Blaber, M., and Strouse, G. F. (2009) Analysis of the dynamics of assembly and structural impact for a histidine tagged FGF1 1.5 nm gold nanoparticle bioconjugate.

Bioconjugate Chem. 20, 2106–2113.

(263)Prasuhn, D. E., Kuzelka, J., Strable, E., Udit, A. K., Cho, S.-H., Lander, G. C., Quispe, J. D., Diers, J. R., Bocian, D. F., Potter, C., Carragher, B., and Finn, M. G. (2008) Polyvalent display of heme on hepatitis B virus capsid protein through coordination to hexahistidine tags. Chem. Biol. 15, 513–519.

(264)Udit, A. K., Hollingsworth, W., and Choi, K. (2010) Metal-

and metallocycle-binding sites engineered into polyvalent virus-like sca olds. Bioconjugate Chem. 21, 399–404.

(265)Kim, M. J., Park, H. Y., Kim, J., Ryu, J., Hong, S., Han, S. J., and

Song, R. (2008) Western blot analysis using metal-nitrilotriacetate conjugated CdSe/ZnS quantum dots. Anal. Biochem. 379, 124–126.

(266)Gupta, M., Caniard, A., Touceda-Varela, A., Campopiano, D. J., and Mareque-Rivas, J. C. (2008) Nitrilotriacetic acid-derivatized quantum dots for simple purification and site-selective fluorescent labeling of active proteins in a single step. Bioconjugate Chem. 19, 1964– 1967.

(267)Bae, P. K., Kim, K. N., Lee, S. J., Chang, H. J., Lee, C. K., and Park, J. K. (2009) The modification of quantum dot probes used for the targeted imaging of his-tagged fusion proteins. Biomaterials 30, 836–842.

(268)Susumu, K., Medintz, I. L., Delehanty, J. B., Boeneman, K., and Mattoussi, H. (2010) Modification of poly(ethylene glycol)-capped quantum dots with nickel nitrilioacetic acid and self-assembly with hisitidine-tagged proteins. J. Phys. Chem. C 114, 13526–13531.

(269)Lee, S. K., Maye, M. M., Zhang, Y. B., Gang, O., and van der Lelie, D. (2009) Controllable g5p-protein-directed aggregatin of ssDNA-gold nanoparticles. Langmuir 25, 657–660.

(270)Gra , R. A., Swanson, T. M., and Strano, M. S. (2008) Synthesis of Ni-NTA coupled single-walled carbon nanotubes for

directed self-assembly with polyhistidine-tagged proteins. Chem. Mater. 20, 1824–1829.

(271)Kim, I., Park, Y. H., Rey, D. A., and Batt, C. A. (2008) Silicadeposited phospholipid nanotubes as a plausible drug targeting system.

J. Drug Targeting 16, 716–722.

(272)Kim, S. H., Jeyakumar, M., and Katzenellenbogen, J. A. (2007) Dual-mode fluorophore-doped nickel nitrilotriacetic acid-modified silica nanoparticles combine histidine-tagged protein purification with sitespecific fluorophore labeling. J. Am. Chem. Soc. 129, 13254–13264.

(273)Xie, H. Y., Zhen, R., Wang, B., Feng, Y. J., Chen, P., and Hao, J. (2010) Fe3O4/Au core/shell nanoparticles modified with Ni2þ-nitri- lotriacetic acid specific to histidine protein. J. Phys. Chem. C 114, 4825–4830.

(274)ShiXing, W., Sun, W., and Zhou, Y. (2010) Preparation of Cu2þ/NTA-derivatized branch polyglycerol magnetic nanoparticles for protein adsorption. J. Nanopart. Res. 12, 2467–2472.

(275)Park, H. Y., Kim, K., Hong, S., Kim, H., Choi, Y., Ryu, J., Kwon, D., Grailhe, R., and Song, R. (2009) Compact and versatile nickel- nitrilotriacetate-modified quantum dots for protein imaging and F€orster resonance energy transfer based assay. Langmuir 26, 7327–7333.

(276)Abad, J. M., Mertens, S. F. L., Pita, M., Fernandez, V. M., and Schi rin, D. J. (2005) Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins.

J. Am. Chem. Soc. 127, 5689–5694.

(277)Yao, H., Zhang, Y., Xiao, F., Xia, Z., and Rao, J. H. (2007) Quantum dot/bioluminescence resonance energy transfer for highly sensitive detection of proteases. Angew. Chem., Int. Ed. 46, 4346–4349.

(278)Boeneman, K., Delehanty, J. B., Susumu, K., Stewart, M. H., and Medintz, I. L. (2010) Intracellular bioconjugation to targeted proteins with semiconductor quantum dots. J. Am. Chem. Soc. 132, 5975–5977.

(279)Sandros, M. G., Gao, D., Gokdemir, C., and Benson, D. E. (2005) General high-a nity approach for the synthesis of fluorophore appended protein nanoparticle assemblies. Chem. Commun. 2832–2834.

(280)Shete, V., and Benson, D. E. (2009) Protein design provides lead(II) ion biosensors for imaging molecular fluxes around red blood cells. Biochemistry 48, 462–470.

(281)Ariyasu, S., Onoda, A., Sakamoto, R., and Yamamura, T. (2009) Alignment of gold clusters on DNA via a DNA-recognizing zinc finger-metallothionein fusion protein. Bioconjugate Chem. 20, 2278– 2285.

(282)Ariyasu, S., Onoda, A., Sakamoto, R., and Yamamura, T. (2009) Conjugation of Au11 cluster with Cys-rich peptides containing the alpha-domain of metallothionein. Dalton Trans. 3742–3747.

(283)Park, T. J., Lee, S. Y., Heo, N. S., and Seo, T. S. (2010) In vivo

synthesis of diverse metal nanoparticles by recombinant Escherichia coli.

Angew. Chem., Int. Ed. 49, 7019–7024.

(284)Gri n, B. A., Adams, S. R., and Tsien, R. Y. (1998) Specific

covalent labeling of recombinant protein molecules inside live cells.

Science 281, 269–272.

(285)Adams, S. R., Campbell, R. E., Gross, L. A., Martin, B. R., Walkup, G. K., Yao, Y., Llopis, J., and Tsien, R. Y. (2002) 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.

(286)Cao, H., Chen, B., Squier, T. C., and Mayer, M. U. (2006) CrAsH: a biarsenical multi-use a nity probe with low non-specific fluorescence. Chem. Commun. 2601–2603.

(287)Genin, E., Carion, O., Mahler, B., Dubertret, B., Arhel, N., Charneau, P., Doris, E., and Mioskowski, C. (2008) CrAsH-quantum dot nanohybrids for smart targeting of proteins. J. Am. Chem. Soc. 130, 8596–8597.

(288)Green, N. M. (1963) Avidin. 1. Use of [14C]Biotin for kinetic studies and for assay. Biochem. J. 89, 585–591.

(289)Schatz, P. J. (1993) Use of peptide libraries to map the substrate-specficity of a peptide-modifying enzyme - A 13 residue consensus peptide specficies biotinylation in Escherichia-coli. Bio-Tech- nology 11, 1138–1143.

(290)Medintz, I. L., Anderson, G. P., Lassman, M. E., Goldman, E. R., Bettencourt, L. A., and Mauro, J. M. (2004) General strategy for biosensor design and construction employing multifunctional surfacetethered components. Anal. Chem. 76, 5620–5629.

(291)Chen, I., Howarth, M., Lin, W. Y., and Ting, A. Y. (2005) Sitespecific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat. Methods 2, 99–104.

(292)O’Hare, H. M., Johnsson, K., and Gautier, A. (2007) Chemical probes shed light on protein function. Curr. Opin. Struct. Biol. 17, 488–494.

(293)Howarth, M., Takao, K., Hayashi, Y., and Ting, A. Y. (2005) Targeting quantum dots to surface proteins in living cells with biotin ligase. Proc. Natl. Acad. Sci. U.S.A 102, 7583–7588.

(294)Chen, I., Choi, Y. A., and Ting, A. Y. (2007) Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins. J. Am. Chem. Soc. 129, 6619–6625.

(295)Sunbul, M., Yen, M., Zou, Y. K., and Yin, J. (2008) Enzyme catalyzed site-specific protein labeling and cell imaging with quantum dots. Chem. Commun. 5927–5929.

(296)Roullier, V., Clarke, S., You, C., Pinaud, F., Gouzer, G., Schaible, D., Marchi-Artzner, V., Piehler, J., and Dahan, M. (2009)

High-a nity labeling and tracking of individual histidine-tagged proteins in live cells using Ni2þ-nitrilotriacetic acid quantum dot conjugates.

Nano Lett. 9, 1228–1234.

(297)Stachler, M. D., Chen, I., Ting, A. Y., and Bartlett, J. S. (2008) Site-specific modification of AAV vector particles with biophysical probes and targeting ligands using biotin ligase. Mol. Ther. 16, 1467–1473.

(298)Maeda, Y., Yoshino, T., Takahashi, M., Ginya, H., Asahina, J., Tajima, H., and Matsunaga, T. (2008) Noncovalent immobilization of streptavidin on in vitroand in vivo-biotinylated bacterial magnetic particles. Appl. Environ. Microbiol. 74, 5139–5145.

(299)George, N., Pick, H., Vogel, H., Johnsson, N., and Johnsson, K. (2004) Specific labeling of cell surface proteins with chemically diverse compounds. J. Am. Chem. Soc. 126, 8896–8897.

(300)Gehring, A. M., Lambalot, R. H., Vogel, K. W., Drueckhammer, D. G., and Walsh, C. T. (1997) Ability of Streptomyces spp acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E-coli holo-ACP synthase. Chem. Biol. 4, 17–24.

(301)Bonasio, R., Carman, C. V., Kim, E., Sage, P. T., Love, K. R., Mempel, T. R., Springer, T. A., and Andrian, U. H. v. (2007) Specific and covalent labeling of a membrane protein with organic fluorochromes and quantum dots. Proc. Natl. Acad. Sci. U.S.A. 104, 14753–14758.

(302)Zheng, M., and Huang, X. Y. (2004) Nanoparticles comprising a mixed monolayer for specific bindings with biomolecules. J. Am. Chem. Soc. 126, 12047–12054.

(303)Terpe, K. (2003) Overview of tag protein fusions: from

molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 60, 523–533.

(304)Los, G. V., Darzins, A., Karassina, N., Zimprich, C., Learish, R., McDougall, M. G., Encell, L. P., Friedman-Ohana, R., Wood, M., Vidugiris, G., Zimmerman, K., Otto, P., Klaubert, D. H., and Wood, K. V. (2005) HaloTag Interchangeable labeling technology for cell imaging and protein capture. Cell Notes 11, 2–6.

(305)Zhang, Y., So, M. K., Loening, A. M., Yao, H. Q., Gambhir, S. S., and Rao, J. H. (2006) HaloTag protein-mediated site-specific conjugation of bioluminescent proteins to quantum dots. Angew. Chem., Int. Ed. 45, 4936–4940.

(306)So, M. K., Yao, H. Q., and Rao, J. H. (2008) HaloTag proteinmediated specific labeling of living cells with quantum dots. Biochem. Biophys. Res. Commun. 374, 419–423.

(307)Bernardes, G. J. L., Chalker, J. M., Errey, J. C., and Davis, B. G. (2008) 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.

(308)Okeley, N. M., Zhu, Y. T., and Donk, W. A. v. d. (2000) Facile chemoselective synthesis of dehydroalanine-containing peptides. Org. Lett. 2, 3603–3606.

(309)Wang, J., Schiller, S. M., and Schultz, P. G. (2007) A Biosynthetic route to dehydroalanine-containing proteins. Angew. Chem., Int. Ed. 46, 6849–6851.

(310)Seebeck, F. P., and Szostak, J. W. (2006) Ribosomal synthesis of dehydroalanine-containing peptides. J. Am. Chem. Soc. 128, 7150–7151.

(311)Dommerholt, J., Schmidt, S., Temming, R., Hendriks, L. J. A., Rutjes, F. P. J. T., Hest, J. C. M. v., Lefeber, D. J., Friedl, P., and van Delft, F. L. (2010) Readily accessible bicyclononynes for bioorthogonal labeling and three-dimensional imaging of living cells. Angew. Chem., Int. Ed. 49, 9422–9425.

(312)Ning, X., Temming, R. P., Dommerholt, J., Guo, J., Ania, D. B., Debets, M. F., Wolfert, M. A., Boons, G. J., and Delft, F. L. v. (2010) Protein modification by strain-promoted alkyne-nitrone cycloaddition.

Angew. Chem., Int. Ed. 49, 3065–3068.

(313)Allen, V. C., Philp, D., and Spencer, N. (2001) Transfer of stereochemical information in a minimal self-replicating system. Org. Lett. 3, 777–780.

(314)Song, W., Wang, J., Qu, J., Madden, M. M., and Lin, Q. (2008) A photoinducible 1,3-dipolar cycloaddition reaction for rapid, selective modification of tetrazole-containing proteins. Angew. Chem., Int. Ed. 47, 2832–2835.

(315)Song, W., Wang, Y., Qu, J., and Lin, Q. (2008) Selective functionalization of a genetically encoded alkene-containing protein via “Photoclick Chemistry” in bacterial cells. J. Am. Chem. Soc. 130, 9654–9655.

(316)Guo, H.-M., Minakawa, M., Ueno, L., and Tanaka, F. (2009) Synthesis and evaluation of a cyclic imine derivative conjugated to a fluorescent molecule for labeling of proteins. Bioorg. Med. Chem. Lett. 19, 1210–1213.

(317)Joshi, N. S., Whitaker, L. R., and Francis, M. B. (2004) A threecomponent Mannich-type reaction for selective tyrosine bioconjugation.

J. Am. Chem. Soc. 126, 15942–15943.

(318)Romanini, D. W., and Francis, M. B. (2007) Attachment of peptide building blocks to proteins through tyrosine bioconjugation.

Bioconjugate Chem. 19, 153–157.

(319)Ban, H., Gavrilyuk, J., and C., F. B., III (2010) Tyrosine

bioconjugation through aqueous ene-type reactions: A click-like reaction for tyrosine. J. Am. Chem. Soc. 132, 1523–1525.

(320)Gilmore, J. M., Scheck, R. A., Esser-Kahn, A. P., Joshi, N. S., and Francis, M. B. (2006) N-Terminal protein modification through a biomimetic transamination reaction. Angew. Chem., Int. Ed. 45, 5307–5311.

(321)Scheck, R. A., Dedeo, M. T., Iavarone, A. T., and Francis, M. B. (2008) Optimization of a biomimetic transamination reaction. J. Am. Chem. Soc. 130, 11762–11770.

(322)Scheck, R. A., and Francis, M. B. (2007) Regioselective labeling of antibodies through N-terminal transamination. ACS Chem. Biol. 2, 247–251.

(323)Lin, Y. A., Chalker, J. M., Floyd, N., Bernardes, G. J. L., and Davis, B. G. (2008) Allyl sulfides are privileged substrates in aqueous

cross-metathesis: Application to site-selective protein modification.

J.Am. Chem. Soc. 130, 9642–9643.

(324)Binder, J. B., and Raines, R. T. (2008) Olefin metathesis for chemical biology. Curr. Opin. Chem. Biol. 12, 767–773.

(325)Lin, Y. A., Chalker, J. M., and Davis, B. G. (2009) Olefin metathesis for site-selective protein modification. ChemBioChem 10, 959–969.

(326)Grubbs, R. H. (2003) Handbook of Metathesis, Wiley-VCH, Weinheim.

(327)Hoveyda, A. H., and Zhugralin, A. R. (2007) The remarkable metal-catalysed olefin metathesis reaction. Nature 450, 243–251.

(328)Alois, F. (2000) Olefin metathesis and beyond. Angew. Chem., Int. Ed. 39, 3012–3043.

(329)Garber, S. B., Kingsbury, J. S., Gray, B. L., and Hoveyda, A. H. (2000) E cient and recyclable monomeric and dendritic Ru-based metathesis catalysts. J. Am. Chem. Soc. 122, 8168–8179.