Poly(ethylene glycol)-supported enzyme inactivators. Efficient identification of the site of covalent attachment to α-chymotrypsin by PEG-TPCK

Bioconjugate Chemistry

Volumn 15, Issue 4, 2004, Pages 673-676

  Schering, Christine A ^a   Zhong, Boyu ^c   Woo, Jonathan C G ^b   Silverman, Richard B ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b ELI LILLY AND COMPANY   (United States)

^c LLC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; ETHYLENE GLYCOL; KETONES; MASS SPECTROMETRY; PEPTIDES; POLYOLS; SYNTHESIS (CHEMICAL); ULTRAVIOLET VISIBLE SPECTROSCOPY;

CHLOROMETHYL; COVALENT ATTACHMENT; EDMAN SEQUENCING; ENZYME INACTIVATION; ISOLATION AND IDENTIFICATION; LABELINGS; PEGYLATED; PROOF OF CONCEPT; SOLUTION-PHASE CHEMISTRY; STANDARD SOLUTIONS;

POLYETHYLENE GLYCOLS;

CHYMOTRYPSIN A; MACROGOL; TOSYLPHENYLALANYL CHLOROMETHYL KETONE;

AQUEOUS SOLUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; COVALENT BOND; EDMAN SEQUENCING; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME MODIFICATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ISOTOPE LABELING; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; METHODOLOGY; PROTEIN DEGRADATION; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; ULTRAVIOLET SPECTROSCOPY;

EID: 3242745982     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc049940p     Document Type: Article

References (25)

1. Suketa, Y., and Inagai, T. (1975) Active site directed inactivators of mouse submaxillary renin. Biochemistry 14 (14), 3188-3194.
2. Delaire, M., Labia, R., Samama, J. P., and Masson, J. M. (1992) Site-directed mutagenesis at the active site of Escherichia coli TEM-1 beta-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis. J. Biol. Chem. 267 (29), 20600-20606.
3. Hubalek, F., Pohl., and Edmondson, D. E. (2003) Structural Comparison of Human Monoamine Oxidases A and B: Mass Spectrometry Monitoring of Cysteine Reactivities. J. Biol. Chem. 278 (31), 28612-28618.
4. McCarter J. D., Burgoyne D. L., Miao S., Zhang S., Callahan J. W., and Withers S. G. (1997) Identification of Glu-268 as the catalytic nucleophile of human lysosomal beta-galactosidase precursor by mass spectrometry. J. Biol. Chem. 272 (1), 396-400.
5. Toy, P. H., and Janda, K. D. (2000) Soluble polymer bound cleavage reagents: a multipolymer strategy for the cleavage of tertiary amines from REM resin. Org. Lett. 2 (15), 2205-2207.
6. Mutter, M., Hagenmaier, H., and Bayer, E. (1971) New method of polypeptide synthesis. Angew. Chem. Int. 10 (11), 811-812.
7. Pillai, V. N. R., Mutter, M. Bayer, E., and Gatfield, I.,(1980) New, easily removable poly(ethylene glycol) supports for the liquid-phase method of peptide synthesis. J. Org. Chem. 45 (26), 5364-5370.
8. Tamada, K., Fujita, E., and Nishimura, S. I. (1998) High performance polymer supports for enzyme-assisted synthesis of glycoconjugates. Carbohydr. Res. 305 (3-4), 443-461.
9. Bonora, G. M. (1987) Use of poly(ethylene glycol) (PEG) as a soluble polymeric support in the oligonucleotide synthesis. A proposal for a new liquid-phase method. Gazz. Chim. Ital. 117 (6), 379-80.
10. Gravert, D. J., and Janda, K. D. (1997) Organic Synthesis on Soluble Polymer Supports: Liquid-Phase Methodologies. Chem. Rev. 97 (2), 489-509.
11. Roberts, M. J., Bentley, M. D., and Harris, J. M. (2002) Chemistry for peptide and protein PEGylation. Adv. Drug Delivery Rev. 54 (4), 459-476.
12. Veronese, F. M. (2001) Peptide and protein PEGylation. A review of problems and solutions. Biomaterials 22 (5), 405-417.
13. Delgado, C., Francis, G. E., and Fisher, D. (1992) The uses and properties of PEG-linked proteins. Crit. Rev. Ther. Drug Carrier Syst. 9 (3-4), 249-304.
14. Matsushima, A., Okada, M., and Inada, Y. (1984) Chymotrypsin modified with poly(ethylene glycol) catalyzes peptide synthesis reaction in benzene. FEBS Lett. 178 (2), 275-277.
15. Pillai, V. N. R., and Mutter, M. (1981) Conformational studies of poly(oxyethylene)-bound peptides and protein sequences. Acc. Chem. Res. 14 (4), 122-130.
16. Hooftman, G., Herman, S., and Schacht, E. J. (1996) Poly-(ethylene glycol)s with reactive end groups. II. Practical consideration for the preparation of protein-PEG conjugates. Bioact. Compatible Polym. 11 (2), 135-159.
17. Drioli, S., Adamo, I., Ballico, M., Morvan, F., and Bonora, G. M. (2002) Liquid-Phase synthesis and characterization of a conjugated chimeric oligonucleotide-PEG-peptide. Eur. J. Org. Chem. (20), 3473-3480.
18. Suzawa, T., Nagamura, S., Saito, H., Ohta, S., Hanai, N., and Yamasaki, M. (2000) Synthesis and HPLC analysis of enzymatically cleavable linker consisting of poly(ethylene glycol) and dipeptide for the development of immunoconjugate. J. Control. Release 69 (1), 27-41.
19. Clark, R., Olson, K., Fuh, G., Marian, M., Mortensen, D., Teshima, G., Chang, S., Chu, H., Mukku, V., Canova-Davis, E., Somers, T., Cronin, M., Winkler, M., and Wells, J. A. (1996) Long-acting growth hormones produced by conjugation with poly(ethylene glycol). J. Biol. Chem. 271 (36), 21969-21977.
20. Schoellmann, G., and Shaw, E. (1963) Direct evidence for the presence of histidine in the active center of chymotrypsin. Biochemistry 2, 252-255.
21. Ong, E. B., Shaw, E., and Schoellmann, G. (1965) The identification of the histidine residue at the active center of chymotrypsin. J. Biol. Chem. 240 (2), 694-698.
22. Kédzy, F. J., Thomson, A., and Bender, M. L. (1967) Reaction of chymotrypsin and L-1-chloro-3-tosylamido-4-phenyl-2-butanone. J. Am. Chem. Soc. 89 (4), 1004-1009.
23. Jameson, G. W., and Elmore, D. T. (1974) Affinity chromatography of bovine trypsin. A rapid separation of bovine alpha- and beta-trypsin. Biochem. J. 141 (2), 555-565.
24. Popenoe, E. A., and du Vigneaud, V. (1954) Synthesis of L-phenylalanyl-L-glutaminyl-L-asparagine. J. Am. Chem. Soc. 76, 6202-6203.
25. Snider, J., Neville, C., Yuan, L. C., and Bullock, J. (1992) Characterization of the heterogeneity of poly(ethylene glycol)-modified superoxide dismutase by chromatographic and electrophoretic techniques. J. Chromatogr. 599 (1-2), 141-55.