Decarboxylative alkylation for site-selective bioconjugation of native proteins via oxidation potentials

Nature Chemistry

Volumn 10, Issue 2, 2018, Pages 205-211

  Bloom, Steven ^a   Liu, Chun ^a   Kölmel, Dominik K ^a   Qiao, Jennifer X ^a,b   Zhang, Yong ^a,b   Poss, Michael A ^a,b   Ewing, William R ^a,b   Macmillan, David W C ^a  

^a PRINCETON UNIVERSITY   (United States)

^b BRISTOL MYERS SQUIBB   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN;

ALKYLATION; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; DECARBOXYLATION; ELECTRON TRANSPORT; LIGHT; MOLECULAR MODEL; OXIDATION REDUCTION REACTION; SYNTHESIS;

ALKYLATION; CATALYSIS; DECARBOXYLATION; ELECTRON TRANSPORT; INSULIN; LIGHT; MODELS, MOLECULAR; MOLECULAR STRUCTURE; OXIDATION-REDUCTION;

EID: 85040991815     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.2888     Document Type: Article

References (47)

1. Boutureira, O. &Bernardes, G. J. L. Advances in chemical protein modification. Chem. Rev. 115, 2174-2195 (2015).
2. Krall, N., da Cruz, F. P., Boutureira, O. &Bernardes, G. J. L. Site-selective protein-modification chemistry for basic biology and drug development. Nat. Chem. 8, 103-113 (2016).
3. Sletten, E. M. &Bertozzi, C. R. Bioorthogonal chemistry: fishing for selectivity in a sea of functionality. Angew. Chem. Int. Ed. 48, 6974-6998 (2009).
4. Saxon, E. &Bertozzi, C. R. Cell surface engineering by a modified Staudinger reaction. Science 287, 2007-2010 (2000).
5. Junutula, J. R. et al. Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index. Nat. Biotechnol. 26, 925-932 (2008).
6. Lyon, R. P., Meyer, D. L., Setter, J. R. &Senter, P. D. Conjugation of anticancer drugs through endogenous monoclonal antibody cysteine resides. Methods Enzymol. 502, 123-138 (2012).
7. Baslé, E., Joubert, N. &Pucheault, M. Protein chemical modification on endogenous amino acids. Chem. Biol. 17, 213-227 (2010).
8. Miller, S., Janin, J., Lesk, A. M. &Chothia, C. Interior and surface of monomeric proteins. J. Mol. Biol. 196, 641-656 (1987).
9. Chen, X., Muthoosamy, K., Pfisterer, A., Neumann, B. &Weil, T. Site-selective lysine modification of native proteins and peptides via kinetically controlled labelling. Bioconjugate Chem. 23, 500-508 (2012).
10. Bader, B. et al. Bioorganic synthesis of lipid-modified proteins for the study of signal transduction. Nature 403, 223-226 (2000).
11. Rosen, C. B. &Francis, M. B. Targeting the N terminus for site-selective protein modification. Nat. Chem. Biol. 13, 697-705 (2017).
12. Romanini, D. W. &Francis, M. B. Attachment of peptide building blocks to proteins through tyrosine bioconjugation. Bioconjugate Chem. 19, 153-157 (2008).
13. Tilley, S. D. &Francis, M. B. Tyrosine-selective protein alkylation using π-allylpalladium complexes. J. Am. Chem. Soc. 128, 1080-1081 (2006).
14. Joshi, N. S., Whitaker, L. R. &Francis, M. B. A three-component Mannich-type reaction for selective tyrosine bioconjugation. J. Am. Chem. Soc. 126, 15942-15943 (2004).
15. Ban, H. et al. Facile and stable linkages through tyrosine: bioconjugation strategies with the tyrosine-click reaction. Bioconjugate Chem. 24, 520-532 (2013).
16. 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).
17. Antos, J. M. &Francis, M. B. Selective tryptophan modification with rhodium carbenoids in aqueous solution. J. Am. Chem. Soc. 126, 10256-10257 (2004).
18. Seki, Y. et al. Transition metal-free tryptophan-selective bioconjugation of proteins. J. Am. Chem. Soc. 138, 10798-10801 (2016).
19. Lin, S. et al. Redox-based reagents for chemoselective methionine bioconjugation. Science 355, 597-602 (2017).
20. Zuo, Z. &MacMillan, D. W. C. Decarboxylative arylation of α-amino acids via photoredox catalysis: a one-step conversion of biomass to drug pharmacophore. J. Am. Chem. Soc. 136, 5257-5260 (2014).
21. Chu, L., Ohta, C., Zuo, Z. &MacMillan, D. W. C. Carboxylic acids as a traceless activation group for conjugate additions: a three-step synthesis of (±)-pregabalin. J. Am. Chem. Soc. 136, 10886-10889 (2014).
22. Noble, A. &MacMillan, D. W. C. Photoredox-mediated α-vinylation of α-amino acids and N-aryl amines. J. Am. Chem. Soc. 136, 11602-11605 (2014).
23. Zuo, Z. et al. Merging photoredox with nickel catalysis: coupling of α-carboxyl sp3-carbons with aryl halides. Science 345, 437-440 (2014).
24. Galicia, M. &González, F. J. Electrochemical oxidation of tetrabutylammonium salts of aliphatic carboxylic acids in acetonitrile. J. Electrochem. Soc. 149, D46-D50 (2002).
25. Hu, Q.-Y., Berti, F. &Adamo, R. Towards the next generation of biomedicines by site-selective conjugation. Chem. Soc. Rev. 45, 1691-1719 (2016).
26. McGrath, N. A., Andersen, K. A., Davis, A. K. F., Lomax, J. E. &Raines, R. T. Diazo compounds for the bioreversible esterification of proteins. Chem. Sci. 6, 752-755 (2015).
27. Rajagopalan, T. G., Stein, W. H. &Moore, S. The inactivation of pepsin by diazoacetylnorleucine methyl ester. J. Biol. Chem. 241, 4295-4297 (1966).
28. Delpierre, G. R. &Fruton, J. S. Specific inactivation of pepsin by a diazo ketone. Proc. Natl Acad. Sci. USA 56, 1817-1822 (1966).
29. Totaro, K. A. et al. Systematic investigation of EDC/sNHS-mediated bioconjugation reactions for carboxylated peptide substrates. Bioconj. Chem. 27, 994-1004 (2016).
30. Noble, A., McCarver, S. J. &MacMillan, D. W. C. Merging photoredox and nickel catalysis: decarboxylative cross-coupling of carboxylic acids with vinyl halides. J. Am. Chem. Soc. 137, 624-627 (2015).
31. Slutskyy, Y. &Overman, L. E. Generation of the methoxycarbonyl radical by visible-light photoredox catalysis and its conjugate addition with electrondeficient olefins. Org. Lett. 18, 2564-2567 (2016).
32. MacDonald, J. I., Munch, H. K., Moore, T. &Francis, M. B. One-step site-specific modification of native proteins with 2-pyridinecarboxyaldehydes. Nat. Chem. Biol. 11, 326-331 (2015).
33. Novak, M., Miller, A., Bruice, T. C. &Tollin, G. The mechanism of flavin 4a substitution which accompanies photolytic decarboxylation of α-substituted acetic acids. Carbanion vs. radical intermediates. J. Am. Chem. Soc. 102, 1465-1467 (1980).
34. Islam, S. D. M., Penzkofer, A. &Hegemann, P. Quantum yield of triplet formation of riboflavin in aqueous solution and of flavin mononucleotide bound to the LOV1 domain of Phot1 from Chlamydomonas reinhardtii. Chem. Phys. 291, 97-114 (2003).
35. Lu, C. et al. Riboflavin (VB2) photosensitized oxidation of 2-deoxyguanosine-5-monophosphate (dGMP) in aqueous solution: a transient intermediates study. Phys. Chem. Chem. Phys. 2, 329-334 (2000).
36. Bortolamei, N., Isse, A. A. &Gennaro, A. Estimation of standard reduction potentials of alkyl radicals involved in atom transfer radical polymerization. Electrochim. Acta 55, 8312-8318 (2010).
37. Huvaere, K. &Skibsted, L. H. Light-induced oxidation of tryptophan and histidine. Reactivity of aromatic N-heterocycles toward triplet-excited flavins. J. Am. Chem. Soc. 131, 8049-8060 (2009).
38. Harriman, A. Further comments on the redox potentials of tryptophan and tyrosine. J. Phys. Chem. 91, 6102-6104 (1987).
39. Stubbe, J. &van der Donk, W. A. Protein radicals in enzyme catalysis. Chem. Rev. 98, 705-762 (1998).
40. Sikorska, E. et al. Spectroscopy and photophysics of lumiflavins and lumichromes. J. Phys. Chem. A 108, 1501-1508 (2004).
41. Koziol, J. Studies on flavins in organic solvents-I. Spectral characteristics of riboflavin, riboflavin tetrabutyrate, and lumichrome. Photochem. Photobiol. 5, 41-54 (1966).
42. Garbaccio, R. M. in Comprehensive Organic Synthesis II 2nd edn, Vol. 1 (eds Knochell, P. &Molander, G. A.) Ch. 9, 438-462 (Elsevier, 2014).
43. Ravelli, D., Zema, M., Mella, M., Fagnoni, M. &Albini, A. Benzoyl radicals from (hetero)aromatic aldehydes. Decatungstate photocatalyzed synthesis of substituted aromatic ketones. Org. Biomol. Chem. 8, 4158-4164 (2010).
44. Wagner, A. &Koniev, O. Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation. Chem. Soc. Rev. 44, 5495-5551 (2015).
45. Uchida, K. &Stadtman, E. R. Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. Proc. Natl Acad. Sci. USA 89, 4544-4548 (1992).
46. Wang, Y., Luo, Y. &Zhang, R. Investigation on insulin tyrosine modification mediated by peroxynitrite. In Proc. IEEE/ICME Int. Conf. Complex Chem. Engineering Beijing, Beijing, 1813-1816 (IEEE, 2007).
47. Lindsay, D. G. &Shall, S. The acetylation of insulin. Biochem. J. 121, 737-745 (1971).