One-step site-specific modification of native proteins with 2-pyridinecarboxyaldehydes

Nature Chemical Biology

Volumn 11, Issue 5, 2015, Pages 326-331

  Macdonald, James I ^a   Munch, Henrik K ^a   Moore, Troy ^a   Francis, Matthew B ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; ENDOCRINE DISRUPTOR; ESTROGEN RECEPTOR; MOLECULAR LIBRARY; PANCREATIC RIBONUCLEASE; PEPTIDE; PICOLINALDEHYDE; PROTEIN; PYRIDINE DERIVATIVE;

BIOTINYLATION; CHEMISTRY; DRUG EFFECTS; HUMAN; MOLECULAR LIBRARY; PROTEIN CONFORMATION;

ALDEHYDES; BIOTINYLATION; ENDOCRINE DISRUPTORS; HUMANS; INDICATORS AND REAGENTS; PEPTIDES; PROTEIN CONFORMATION; PROTEINS; PYRIDINES; RECEPTORS, ESTROGEN; RIBONUCLEASE, PANCREATIC; SMALL MOLECULE LIBRARIES;

EID: 84932182042     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1792     Document Type: Article

References (50)

1. Hermanson, G.T. Bioconjugate Techniques (Academic Press, San Diego, CA, 1996).
2. Griffin, B.A., Adams, S.R. & Tsien, R.Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272 (1998).
3. Zalipsky, S. Functionalized poly(ethylene glycols) for preparation of biologically relevant conjugates. Bioconjug. Chem. 6, 150-165 (1995).
4. Rao, J., Dragulescu-Andrasi, A. & Yao, H. Fluorescence imaging in vivo: Recent advances. Curr. Opin. Biotechnol. 18, 17-25 (2007).
5. Witus, L.S. & Francis, M.B. Using synthetically modified proteins to make new materials. Acc. Chem. Res. 44, 774-783 (2011).
6. Szobota, S. et al. Remote control of neuronal activity with a light-gated glutamate receptor. Neuron 54, 535-545 (2007).
7. 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).
8. 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).
9. Van Hest, J.C.M., Kiick, K.L. & Tirrell, D.A. Efficient incorporation of unsaturated methionine analogues into proteins in vivo. J. Am. Chem. Soc. 122, 1282-1288 (2000).
10. Dawson, P.E., Muir, T., Clark-Lewis, I. & Kent, S. Synthesis of proteins by native chemical ligation. Science 266, 776-779 (1994).
11. Muir, T.W. Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 72, 249-289 (2003).
12. Wu, P. et al. Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag. Proc. Natl. Acad. Sci. USA 106, 3000-3005 (2009).
13. Uttamapinant, C. et al. A fluorophore ligase for site-specific protein labeling inside living cells. Proc. Natl. Acad. Sci. USA 107, 10914-10919 (2010).
14. Baker, D.P. et al. N-terminally PEGylated human interferon-?-1a with improved pharmacokinetic properties and in vivo efficacy in a melanoma angiogenesis model. Bioconjug. Chem. 17, 179-188 (2006).
15. Singudas, R., Adusumalli, S.R., Joshi, P.N. & Rai, V. A phthalimidation protocol that follows protein defined parameters. Chem. Commun. (Camb.) 51, 473-476 (2015).
16. Chan, A.O.Y. et al. Modification of N-terminal ?-amino groups of peptides and proteins using ketenes. J. Am. Chem. Soc. 134, 2589-2598 (2012).
17. Tam, J.P., Yu, Q. & Miao, Z. Orthogonal ligation strategies for peptide and protein. Biopolymers 51, 311-332 (1999).
18. 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).
19. Ning, X. et al. Protein modification by strain-promoted alkyne-nitrone cycloaddition. Angew. Chem. Int. Ed. Engl. 49, 3065-3068 (2010).
20. Li, X., Zhang, L., Hall, S.E. & Tam, J.P. A new ligation method for N-terminal tryptophan-containing peptides using the Pictet-Spengler reaction. Tetrahedr. Lett. 41, 4069-4073 (2000).
21. 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. Engl. 45, 5307-5311 (2006).
22. Witus, L.S. et al. Site-specific protein transamination using N-methylpyridinium-4-carboxaldehyde. J. Am. Chem. Soc. 135, 17223-17229 (2013).
23. Dixon, H.B.F. & Fields, R. Specific modification of NH2-terminal residues by transamination. Methods Enzymol. 25, 409-419 (1972).
24. Dixon, H.B.F. N-terminal modification of proteins-A review. J. Protein Chem. 3, 99-108 (1984).
25. Obermeyer, A.C., Jarman, J.B. & Francis, M.B. N-terminal modification of proteins with o-aminophenols. J. Am. Chem. Soc. 136, 9572-9579 (2014).
26. Baldwin, J.E. Rules for ring closure. J. Chem. Soc. Chem. Commun. 734-736 (1976).
27. San George, R.C. & Hoberman, H.D. Reaction of acetaldehyde with hemoglobin. J. Biol. Chem. 261, 6811-6821 (1986).
28. Metz, B. et al. Identification of formaldehyde-induced modifications in proteins: Reactions with model peptides. J. Biol. Chem. 279, 6235-6243 (2004).
29. Fraenkel-Conrat, H. & Olcott, H.S. Reaction of formaldehyde with proteins: VI. Cross-linking of amino groups with phenol, imidazole, or indole groups. J. Biol. Chem. 174, 827-843 (1948).
30. Join, B. et al. Selective iron-catalyzed oxidation of benzylic and allylic alcohols. Adv. Synth. Catal. 353, 3023-3030 (2011).
31. Storr, T. et al. Ru(iii) complexes of Edta and Dtpa polyaminocarboxylate analogues and their use as nitric oxide scavengers. Eur. J. Inorg. Chem. 2005, 2685-2697 (2005).
32. Gaertner, H.F. & Offord, R.E. Site-specific attachment of functionalized poly(ethylene glycol) to the amino terminus of proteins. Bioconjug. Chem. 7, 38-44 (1996).
33. Peter, W. et al. Interchain cysteine bridges control entry of progesterone to the central cavity of the uteroglobin dimer. Protein Eng. 5, 351-359 (1992).
34. Glazer, A.N. Specific chemical modification of proteins. Annu. Rev. Biochem. 39, 101-130 (1970).
35. Anderson, P.J. & Perham, R.N. The reactivity of thiol groups and the subunit structure of aldolase. Biochem. J. 117, 291-298 (1970).
36. Joo, C., Balci, H., Ishitsuka, Y., Buranachai, C. & Ha, T. Advances in single-molecule fluorescence methods for molecular biology. Annu. Rev. Biochem. 77, 51-76 (2008).
37. Witus, L.S. et al. Identification of highly reactive sequences for PLP-mediated bioconjugation using a combinatorial peptide library. J. Am. Chem. Soc. 132, 16812-16817 (2010).
38. Wiita, A.P., Hsu, G.W., Lu, C.M., Esensten, J.H. & Wells, J.A. Circulating proteolytic signatures of chemotherapy-induced cell death in humans discovered by N-terminal labeling. Proc. Natl. Acad. Sci. USA 111, 7594-7599 (2014).
39. Diamanti-Kandarakis, E. et al. Endocrine-disrupting chemicals: An endocrine society scientific statement. Endocr. Rev. 30, 293-342 (2009).
40. Ternes, T.A. et al. Ozonation: A tool for removal of pharmaceuticals, contrast media and musk fragrances from wastewater? Water Res. 37, 1976-1982 (2003).
41. Blair, R.M. et al. The estrogen receptor relative binding affinities of 188 natural and xenochemicals: Structural diversity of ligands. Toxicol. Sci. 54, 138-153 (2000).
42. Gangloff, M. et al. Crystal structure of a mutant hER? ligand-binding domain reveals key structural features for the mechanism of partial agonism. J. Biol. Chem. 276, 15059-15065 (2001).
43. Gryder, B.E. et al. Histone deacetylase inhibitors equipped with estrogen receptor modulation activity. J. Med. Chem. 56, 5782-5796 (2013).
44. Himo, F. et al. Copper(i)-catalyzed synthesis of azoles. DFT study predicts unprecedented reactivity and intermediates. J. Am. Chem. Soc. 127, 210-216 (2004).
45. Cecconi, C., Shank, E.A., Bustamante, C. & Marqusee, S. Direct observation of the three-state folding of a single protein molecule. Science 309, 2057-2060 (2005).
46. Banerjee, D., Liu, A.P., Voss, N.R., Schmid, S.L. & Finn, M.G. Multivalent display and receptor-mediated endocytosis of transferrin on virus-like particles. ChemBioChem 11, 1273-1279 (2010).
47. 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 Nano 4, 6014-6020 (2010).
48. Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970).
49. Wang, H. et al. Self-assembled nanospheres as a novel delivery system for taxol: A molecular hydrogel with nanosphere morphology. Chem. Commun. (Camb.) 47, 4439-4441 (2011).
50. Van Gompel, J. & Schuster, G.B. Chemiluminescence of organic peroxides: Intramolecular electron-exchange luminescence from a secondary perester. J. Org. Chem. 52, 1465-1468 (1987).