Modification of amino groups

Current Protocols in Protein Science

Volumn 2016, Issue , 2016, Pages 15.2.1-15.2.20

  Geoghegan, Kieran F ^a  

^a PFIZER INC   (United States)

Author keywords

Amino group; Chemical modification; Crystallization; Reductive alkylation; Succinimidyl ester

Indexed keywords

ALPHA AMINO ACID; AMINO ACID; AMINOACYLTRANSFERASE; BIOTIN; CYSTEINE; FLUORESCEIN ISOTHIOCYANATE; N HYDROXYSUCCINIMIDE; REAGENT; SERINE; SUCCINIMIDE DERIVATIVE; SUCCINIMIDYL ESTER; THREONINE; UNCLASSIFIED DRUG; FLUORESCENT DYE; PEPTIDE; PROTEIN; SUCCINIMIDYL ACETATE;

ACYLATION; ALKYLATION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; ARYLATION; BIOTINYLATION; CARBAMOYLATION; CATALYSIS; CHEMICAL MODIFICATION; CHEMICAL REACTION; CROSS LINKING; METHYLATION; OXIDATION; PH; PRIORITY JOURNAL; PROTEIN STRUCTURE; TRANSAMINATION; CHEMISTRY; OXIDATION REDUCTION REACTION;

ALKYLATION; AMINO ACIDS; FLUORESCEIN-5-ISOTHIOCYANATE; FLUORESCENT DYES; OXIDATION-REDUCTION; PEPTIDES; PROTEINS; SUCCINIMIDES;

EID: 85011662528     PISSN: 19343655     EISSN: 19343663     Source Type: Journal    
DOI: 10.1002/cpps.17     Document Type: Article

References (42)

1. Aitken, A. and Learmonth, M. 2002. Succinylation of proteins. In The Protein Protocols Handbook (J.M. Walker, ed.) pp. 459-460. Humana Press, Totowa, N.J. doi: 10.1385/1-59259-169-8:459.
2. Banks, P.R. and Paquette, D.M. 1995. Comparison of three common amine reactive fluorescent probes used for conjugation to biomolecules by capillary zone electrophoresis. Bioconjug. Chem. 6:447-458. doi: 10.1021/bc00034a015.
3. Beckett, D., Kovaleva, E., and Schatz, P.J. 1999. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8:921-929. doi: 10.1110/ps.8.4.921.
4. Bernardes, G.J.L., Steiner, M., Hartmann, I., Neri, D., and Casi, G. 2013. Site-specific chemical modification of antibody fragments using traceless cleavable linkers. Nat. Protoc. 8:2079-2089. doi: 10.1038/nprot.2013.121.
5. Borch, R.F., Bernstein, M.D., and Durst, H.D. 1971. Cyanohydridoborate anion as a selective reducing agent. J. Am. Chem. Soc. 93:2897-2904. doi: 10.1021/ja00741a013.
6. Bunton, C.A., Fuller, N.A., Perry, S.G., and Shiner, V.J., Jr. 1963. The hydrolysis of carboxylic anhydrides. III. Reactions in initially neutral solution. J. Chem. Soc. 2918-2926. doi: 10.1039/jr9630002918.
7. Cohen-Hadar, N., Lagziel-Simis, S., Wine, Y., Frolow, F., and Freeman, A. 2010. Restructuring protein crystals porosity for biotem-plating by chemical modification of lysine residues. Biotechnol. Bioeng. 108:1-11. doi: 10.1002/bit.22921.
8. da Silva Freitas, D., Mero, A., and Pasut, G. 2013. Chemical and enzymatic site specific PEGylation of hGH. Bioconjug. Chem. 24:456-463. doi: 10.1021/bc300594y.
9. Gaertner, H.F. and Offord, R.E. 1996. Site-specific attachment of functionalized poly(ethylene glycol) to the amino terminus of proteins. Biocon-jug. Chem. 7:38-44. doi: 10.1021/bc950074d.
10. Gaertner, H.F., Rose, K., Cotton, R., Timms, D., Camble, R., and Offord, R.E. 1992. Construction of protein analogs by site-specific condensation of unprotected fragments. Bioconjug. Chem. 3:262-268. doi: 10.1021/bc00015a010.
11. Geoghegan, K.F. and Stroh, J.G. 1992. 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. doi: 10.1021/bc00014a008.
12. Geoghegan, K.F., Dixon, H.B., Rosner, P.J., Hoth, L.R., Lanzetti, A.J., Borzilleri, K.A., Marr, E.S., Pezzullo, L.H., Martin, L.B., LeMotte, P.K., Mc-Coll, A.S., Kamath, A.V., and Stroh, J.G. 1999. Spontaneous a-N-6-phosphogluconoylation of a “His tag” in Escherichia coli: The cause of extra mass of 258 or 178 Da in fusion proteins. Anal. Biochem. 267:169-184. doi: 10.1006/abio.1998.2990.
13. Kalkhof, S. and Sinz, A. 2008. Chances and pitfalls of chemical cross-linking with amine-reactive N-hydroxysuccinimide esters. Anal. Bioanal. Chem. 392:305-312. doi: 10.1007/s00216-008-2231-5.
14. Kim, Y., Quartey, P., Li, H., Volkart, L., Hat-zos, C., Chang, C., Nocek, B., Cuff, M., Os-ipiuk, J., Tan, K., Fan, Y., Bigelow, L., Malt-seva, N., Wu, R., Borovilos, M., Duggan, E., Zhou, M., Binkowski, T.A., Zhang, R.-g., and Joachimiak, A. 2008. Large-scale evaluation of protein reductive methylation for improving protein crystallization. Nat. Methods 5:853-854. doi: 10.1038/nmeth1008-853.
15. Kinstler, O., Molineux, G., Treuheit, M., Ladd, D., and Gegg, C. 2002. Mono-N-terminal poly(ethylene glycol)-protein conjugates. Adv. Drug Deliv. Rev. 54:477-485. doi: 10.1016/S0169-409X(02)00023-6.
16. Koniev, O. and Wagner, A. 2015. Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation. Chem. Soc. Rev. 44:5495-5551. doi: 10.1039/C5CS00048C.
17. Korzhavin, D.V., Chernovskaya, T.V., Efanov, Y.G., Rudenko, E.G., Ivanov, R.A., Pshenichnikova, A.B., and Shvets, V.I. 2015. Preparation of monoPEGylated human interferon beta-1a: Optimization of the conditions for N-terminal PE-Gylation. Appl. Biochem. Microbiol. 51:774-785. doi: 10.1134/S0003683815070030.
18. Larda, S.T., Pichugin, D., and Prosser, R.S. 2015. Site-specific labeling of protein lysine residues and N-terminal amino groups with in-doles and indole-derivatives. Bioconjug. Chem. 26:2376-2383. doi: 10.1021/acs.bioconjchem.5b00457.
19. Leitner, A., Walzthoeni, T., and Aebersold, R. 2014. Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline. Nat. Protoc. 9:120-137. doi: 10.1038/nprot.2013.168.
20. Liu, X. and Reilly, J.P. 2009. Correlating the chemical modification of Escherichia coli ri-bosomal proteins with crystal structure data. J. Proteome Res. 8:4466-4478. doi: 10.1021/pr9002382.
21. Matsumoto, M., Nakagawa, T., Uchida, Y., Seki, K., Ohba, M., and Kondo, K. 2016. Effect of modification of citraconic anhydrides on catalytic activity and thermostability of enzymes. J. Chem. Technol. Biotechnol. 91:59-64. doi: 10.1002/jctb.4556.
22. Mindt, T.L., Jungi, V., Wyss, S., Friedli, A., Pla, G., Novak-Hofer, I., Grunberg, J., and Schibli, R. 2008. Modification of different IgG1 antibodies via glutamine and lysine using bacterial and human tissue transglutaminase. Bioconjug. Chem. 19:271-278. doi: 10.1021/bc700306n.
23. Minguez, P., Parca, L., Diella, F., Mende, D.R., Kumar, R., Helmer-Citterich, M., Gavin, A.C., van Noort, V., and Bork, P. 2012. Deciphering a global network of functionally associated post-translational modifications. Mol. Syst. Biol. 8:599. doi: 10.1038/msb.2012.31.
24. Narayanan, A. and Jones, L.H. 2015. Sulfonyl fluorides as privileged warheads in chemical biology. Chem. Sci. 6:2650-2659. doi: 10.1039/C5SC00408J.
25. Ouellette, D., Alessandri, L., Chin, A., Grinnell, C., Tarcsa, E., Radziejewski, C., and Correia, I. 2010. Studies in serum support rapid formation of disulfide bond between unpaired cysteine residues in the VH domain of an immunoglobu-lin G1 molecule. Anal. Biochem. 397:37-47. doi: 10.1016/j.ab.2009.09.027.
26. Palla, K.S., Witus, L.S., Mackenzie, K.J., Netirojjanakul, C., and Francis, M.B. 2015. Optimization and expansion of a site-selective N-methylpyridinium-4-carboxaldehyde-mediated transamination for bacterially expressed proteins. J. Am. Chem. Soc. 137:1123-1129. doi: 10.1021/ja509955n.
27. Patricelli, M.P., Szardenings, A.K., Liyanage, M., Nomanbhoy, T.K., Wu, M., Weissig, H., Aban, A., Chun, D., Tanner, S., and Kozarich, J.W. 2007. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry 46:350-358. doi: 10.1021/bi062142x.
28. Pauillac, S., Naar, J., Mouratou, B., and Gues-don, J.-L. 2002. Application of a modified version of Habeeb’s trinitrophenylation method for the characterization of hapten-protein conjugates in a reversed micellar medium. J. Immunol. Methods 263:75-83. doi: 10.1016/S0022-1759(02)00039-X.
29. 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. doi: 10.1021/ja802495w.
30. Spicer, C.D. and Davis, B.G. 2014. Selective chemical protein modification. Nat. Commun. 5:4740. doi: 10.1038/ncomms5740.
31. Starheim, K.K., Gevaert, K., and Arnesen, T. 2012. Protein N-terminal acetyltransferases: When the start matters. Trends Biochem. Sci. 37:152-161. doi: 10.1016/j.tibs.2012.02.003.
32. Sutherland, B.W., Toews, J., and Kast, J. 2008. Utility of formaldehyde cross-linking and mass spectrometry in the study of protein-protein interactions. J. Mass Spectrom. 43:699-715. doi: 10.1002/jms.1415.
33. Tan, K., Kim, Y., Hatzos-Skintges, C., Chang, C., Cuff, M., Chhor, G., Osipiuk, J., Michalska, K., Nocek, B., An, H., Babnigg, G., Bigelow, L., Joachimiak, G., Li, H., Mack, J., Makowska-Grzyska, M., Maltseva, N., Mulligan, R., Tesar, C., Zhou, M., and Joachimiak, A. 2014. Salvage of failed protein targets by reductive alky-lation. In Methods in Molecular Biology, vol. 1140, pp. 189-200. Springer, New York. doi: 10.1007/978-1-4939-0354-2_15.
34. Wagner, A.M., Fegley, M.W., Warner, J.B., Grind-ley, C.L.J., Marotta, N.P., and Petersson, E.J. 2011. N-Terminal protein modification using simple aminoacyl transferase substrates. J. Am. Chem. Soc. 133:15139-15147. doi: 10.1021/ja2055098.
35. Walter, T.S., Meier, C., Assenberg, R., Au, K.-F., Ren, J., Verma, A., Nettleship, J.E., Owens, R.J., Stuart, D.I., and Grimes, J.M. 2006. Lysine methylation as a routine rescue strategy for protein crystallization. Structure 14:1617-1622. doi: 10.1016/j.str.2006.09.005.
36. Wetzel, R., Halualani, R., Stults, J.T., and Quan, C. 1990. A general method for highly selective cross-linking of unprotected polypeptides via pH-controlled modification of N-terminal α-amino groups. Bioconjug. Chem. 1:114-122. doi: 10.1021/bc00002a005.
37. Witus, L.S. and Francis, M. 2010. Site-specific protein bioconjugation via a pyridoxal 5 -phosphate-mediated N-terminal transamination reaction. Curr. Protoc. Chem. Biol. 2:125-134. doi: 10.1002/9780470559277.ch100018.
38. Zhang, L. and Tam, J.P. 1996. Thiazolidine formation as a general and site-specific conjugation method for synthetic peptides and proteins. Anal. Biochem. 233:87-93. doi: 10.1006/abio.1996.0011.
39. Zhao, Z.G., Im, J.S., Lam, K.S., and Lake, D.F. 1999. Site-specific modification of a single-chain antibody using a novel glyoxylyl-based labeling reagent. Bioconjug. Chem. 10:424-430. doi: 10.1021/BC980120K.
40. Koniev, O. and Wagner, A. 2015. See above. An excellent overview of chemical modification of proteins, and good on all aspects of amino group modification.
41. The Molecular Probes Handbook—A Guide to Fluorescent Probes and Labeling, 11th ed. 2010. (ThermoFisher Scientific).
42. Earlier editions of this commercially supported resource were authored by R. P. Haugland. It is a long-standing and valuable resource for all aspects of chemical modification related to the incorporation of dyes, biotin, and other reporter groups into proteins and other biomolecules.