Effects of antioxidants on the hydrogen peroxide-mediated oxidation of methionine residues in granulocyte colony-stimulating factor and human parathyroid hormone fragment 13-34

Pharmaceutical Research

Volumn 21, Issue 12, 2004, Pages 2377-2383

  Yin, Jin ^a   Chu, Jhih Wei ^a   Ricci, Margaret Speed ^b   Brems, David N ^b   Wang, Daniel I C ^a   Trout, Bernhardt L ^a  

^a Massachusetts Institute of Technology Cambridge   (United States)

^b AMGEN INC   (United States)

Author keywords

Antioxidants; Ascorbic acid; Granulocyte colony stimulating factor (G CSF); Human parathyroid hormone (hPTH); Methionine oxidation

Indexed keywords

ACETYLCYSTEINE; ANTIOXIDANT; EDETIC ACID; GLUTATHIONE; GRANULOCYTE COLONY STIMULATING FACTOR; HYDROGEN PEROXIDE; HYDROXYL RADICAL; METAL ION; METHIONINE; PARATHYROID HORMONE; PARATHYROID HORMONE[13-34]; PEPTIDE FRAGMENT; SCAVENGER; TRANSITION ELEMENT; UNCLASSIFIED DRUG;

ACIDITY; ALKALINITY; ARTICLE; CHEMICAL ENGINEERING; COMPLEX FORMATION; CONCENTRATION PROCESS; DEGRADATION KINETICS; DRUG EFFICACY; ELIMINATION REACTION; FENTON REACTION; OXIDATION; OXIDATION KINETICS; PEPTIDE ANALYSIS; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN ENGINEERING; QUANTITATIVE ANALYSIS; REACTION ANALYSIS; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;

ANTIOXIDANTS; DOSE-RESPONSE RELATIONSHIP, DRUG; GRANULOCYTE COLONY-STIMULATING FACTOR; HUMANS; HYDROGEN PEROXIDE; METHIONINE; OXIDATION-REDUCTION; PARATHYROID HORMONE; PEPTIDE FRAGMENTS;

EID: 17644401767     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11095-004-7692-4     Document Type: Article

References (37)

1. S. H. Li, C. Schöneich, and R. T. Borchardt. Chemical-instability of protein pharmaceuticals - mechanisms of oxidation and strategies for stabilization. Biotechnol. Bioeng. 48:490-500 (1995).
2. W. Wang. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int. J. Pharm. 185:129-188 (1999).
3. Y. Nabuchi, E. Fujiwara, K. Ueno, H. Kuboniwa, Y. Asoh, and H. Ushio. Oxidation of recombinant human parathyroid hormone: Effect of oxidized position on the biological activity. Pharm. Res. 12:2049-2052 (1995).
4. S. W. Griffiths and C. L. Cooney. Relationship between protein structure and methionine oxidation in recombinant human alpha 1-antitrypsin. Biochemistry 41:6245-6252 (2002).
5. S. M. Van Patten, E. Hanson, R. Bernasconi, K. Zhang, P. Manavalan, E. S. Cole, J. M. McPherson, and T. Edmunds. Oxidation of methionine residues in antithrombin - Effects on biological activity and heparin binding. J. Biol. Chem. 274:10268-10276 (1999).
6. E. T. Duenas, R. Keck, A. De Vos, A. J. S. Jones, and J. L. Cleland. Comparison between light induced and chemically induced oxidation of rhVEGF. Pharm. Res. 18:1455-1460 (2001).
7. J. L. Liu, K. V. Lu, T. Eris, V. Katta, K. R. Westcott, L. O. Narhi, and H. S. Lu, In vitro methionine oxidation of recombinant human leptin. Pharm. Res. 15:632-640 (1998).
8. H. S. Lu, P. R. Fausset, L. O. Narhi, T. Horan, K. Shinagawa, G. Shimamoto, and T. C. Boone. Chemical modification and site-directed mutagenesis of methionine residues in recombinant human granulocyte colony-stimulating factor: effect on stability and biological activity. Arch. Biochem. Biophys. 362:1-11 (1999).
9. J. L. Cleland and R. Langer. Formulation and delivery of proteins and peptides - design and development strategies. ACS Sym. Ser 567:1-19 (1994).
10. T. Osterberg and A. Fatouros. Oxygen-reduced aqueous solution of factor VIII. U.S. Patent No. 5,962,650 (1999)
11. T. Osterberg and A. Fatouros. Protein formulation comprising coagulation factor VIII or factor IX in an aqueous solution. U.S. Patent No. 5,919,908 (1999)
12. S. H. Li, C. Schöneich, and R. T. Borchardt. Chemical pathways of peptide degradation. VIII. Oxidation of methionine in small model peptides by prooxidant/transition metal ion systems: influence of selective scavengers for reactive oxygen intermediates. Pharm. Res. 12:348-355 (1995).
13. V. M. Knepp. J. L. Whatley. A. Muchnik, and T. S. Calderwood. Identification of antioxidants for prevention of peroxide-mediated oxidation of recombinant human ciliary neurotrophic factor and recombinant human nerve growth factor. PDA J. Pharm. Sci. Technol. 50(3):163-171 (1996).
14. X. M. Lam, J. Y. Yang, and J. L. Cleland. Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2. J. Pharm. Sci. 86:1250-1255 (1997).
15. J. A. Cadee, M. J. van Steenbergen, C. Versluis, A. J. R. Heck, W. J. M. Underberg, W. den Otter, W. Jiskoot, and W. E. Hennink. Oxidation of recombinant human interleukin-2 by potassium peroxodisulfate. Pharm. Res. 18:1461-1467 (2001).
16. S. H. Li, C. Schöneich, G. S. Wilson, and R. T. Borchardt. Chemical pathways of peptide degradation. V. ascorbic-acid promotes rather than inhibits the oxidation of methionine to methionine sulfoxide in small model peptides. Pharm. Res. 10:1572-1579 (1993).
17. J. C. Deutsh. Ascorbic acid oxidation of hydrogen peroxide. Anal. Biochem. 255:1-7 (1998).
18. B. Bishop, D. C. Koay, A. C. Sartorelli, and L. Regan. Reengineering granulocyte colony-stimulating factor for enhanced stability. J. Biol. Chem. 276:33465-33470 (2001).
19. J.-W. Chu, J. Yin, D. I. C. Wang, and B. L. Trout. Molecular dynamics and oxidation rates of methionine residues of granulocyte colony-stimulating factor (G-CSF) at different pH values. Biochemistry 43:1019-1029 (2004).
20. A. L. Frelinger and J. E. Zull. Oxidized forms of parathyroid-hormone with biological-activity - separation and characterization of hormone forms oxidized at methionine-8 and methionine - 18. J. Biol. Chem. 259:5507-5513 (1984).
21. Available at: http://www.rxlist.com/cgi/generic/filgrastim.htm (accessed 4/27/2004).
22. S. P. Wolff. Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. Method. Enzymol. 233:182-189 (1994).
23. C. C. Winterbourn and D. Metodiewa. Reactivity of biologically important thiol compounds with Superoxide and hydrogen peroxide. Free Radical Bio. Med. 27:322-328 (1999).
24. J. C. Deutsh. Oxygen-accepting antioxidants which arise during ascorbate oxidation. Anal. Biochem. 265:238-245 (1998).
25. J. C. Deutsh. Dehydroascorbic acid. J. Chromatogr. A. 881:299-307 (2000).
26. P. Wardman and L. P. Candeias. Fenton chemistry: an introduction. Radiat. Res. 145:523-531 (1996).
27. M. J. Burkitt and B. C. Gilbert. Model studies of the iron-catalysed Haber-Weiss cycle and the ascorbate-driven Fenton reation. Free Radical Res. Com. 10:265-280 (1990).
28. M. J. Zhao and L. Jung. Kinetics of the competitive degradation of deoxyribose and other molecules by hydroxyl radicals produced by the Fenton reaction in the presence of ascorbic-acid. Free Radic. Res. 23:229-243 (1995).
29. G. R. Buettner and B. A. Jurkiewicz. Catalytic metals, ascorbate and free radicals: combinations to avoid. Radiat. Res. 145:532-541 (1996).
30. J. E. Biaglow, Y Manevich, F. Uckun, and K.D. Held. Quantitation of hydroxyl radicals produced by radiation and copper-linked oxidation of ascorbate by 2-deoxy-D-ribose method. Free Radical Bio. Med. 22:1129-1138 (1997).
31. A. Rees and T. F. Slater. Ascorbic acid and lipid peroxidation: the cross-over effect. Acta Biochim. Biophys. 22:241-249 (1987).
32. L. Packer and J. Fuchs. Health and Disease, Marcel Dekker Inc., New York, 1997, pp. 75-94
33. G. R. Buettner. In the absence of catalytic metals ascorbate does not autoxidize at pH 7: ascorbate as a test for catalytic metals. J. Biochem. Biophys. Methods 16:27-40 (1988).
34. G. R. Buettner, T. P. Doherty, and L. K. Patterson. The kinetics of the reaction of superoxide radical with Fe(III) complexes of EDTA, DETAPAC and HEDTA. FEBS Lett. 158:143-146 (1983).
35. J. Butler and B. Halliwell. Reaction of iron EDTA chelates with the superoxide radical. Arch. Biochem. Biophys. 218:174-178 (1982).
36. K. D. Welch, T. Z. Davis, and S. D. Aust. Iron autoxidation and free radical generation: effects of buffers, ligands, and chelators. Arch. Biochem. Biophys. 397:360-369 (2002).
37. J. Van der Zee and P. J. A. Van den Broek. Determination of the ascorbate free radical concentration in mixtures of ascorbate and dehydroascorbate. Free Radical Bio. Med. 25:282-286 (1998).