Comparison of the oxidative folding of lysozyme at a high protein concentration using aromatic thiols versus glutathione

Journal of Biotechnology

Volumn 142, Issue 3-4, 2009, Pages 214-219

  Madar, David J ^a   Patel, Amar S ^a   Lees, Watson J ^a  

^a FLORIDA INTERNATIONAL UNIVERSITY   (United States)

Author keywords

Lysozyme; Protein folding kinetic; Protein renaturation; Redox buffer

Indexed keywords

AROMATIC DISULFIDES; AROMATIC THIOL; GLUTATHIONE; GLUTATHIONE DISULFIDE; IN-VITRO; LYSOZYME; OXIDATIVE FOLDING; PROTEIN CONCENTRATIONS; PROTEIN FOLDING KINETIC; PROTEIN PRODUCTION; RECOMBINANT DNA TECHNOLOGY; REDOX BUFFER; SMALL MOLECULES;

AROMATIC COMPOUNDS; AROMATIZATION; DNA; ENZYMES; GENETIC ENGINEERING; KINETIC ENERGY; NUCLEIC ACIDS; RATE CONSTANTS;

PROTEIN FOLDING;

BUFFER; DISULFIDE; GLUTATHIONE; GLUTATHIONE DISULFIDE; LYSOZYME; THIOL;

ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; IN VITRO STUDY; OXIDATION; OXIDATION REDUCTION STATE; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SYNTHESIS; RECOMBINANT DNA TECHNOLOGY;

ANIMALS; CHICKENS; DISULFIDES; GLUTATHIONE; GUANIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MURAMIDASE; PROTEIN FOLDING; PROTEIN RENATURATION; SULFHYDRYL COMPOUNDS;

EID: 67650045986     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2009.05.003     Document Type: Article

References (53)

1. Acharya A.S., and Taniuchi H. Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation. Mol. Cell Biochem. 44 (1982) 129-148
2. Arakawa T., and Tsumoto K. The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem. Biophys. Res. Commun. 304 (2003) 148-152
3. Bach R.D., Dmitrenko O., and Thorpe C. Mechanism of thiolate-disulfide interchange reactions in biochemistry. J. Org. Chem. 73 (2008) 12-21
4. Creighton T.E., Zapun A., and Darby N.J. Mechanisms and catalysts of disulfide bond formation in proteins. Trends Biotechnol. 13 (1995) 18-23
5. De Bernardez Clark E., Schwarz E., and Rudolph R. Inhibition of aggregation side reactions during in vitro protein folding. Method Enzymol. 309 (1999) 217-236
6. DeCollo T.V., and Lees W.J. Effects of aromatic thiols on thiol-disulfide interchange reactions that occur during protein folding. J. Org. Chem. 66 (2001) 4244-4249
7. Dobson C.M., Evans P.A., and Radford S.E. Understanding how proteins fold: the lysozyme story so far. Trends Biochem. Sci. 19 (1994) 31-37
8. Dong X.-Y., Huang Y., and Sun Y. Refolding kinetics of denatured-reduced lysozyme in the presence of folding aids. J. Biotechnol. 114 (2004) 135-142
9. Epstein C.J., and Goldberger R.F. Factors influencing the reactivation of reduced egg white lysozyme. J. Biol. Chem. 238 (1963) 1380-1383
10. Expert-Bezancon N., Rabilloud T., Vuillard L., and Goldberg M.E. Physical-chemical features of non-detergent sulfobetaines active as protein-folding helpers. Biophys. Chem. 100 (2003) 469-479
11. Georgiou G., and Valax P. Isolating inclusion bodies from bacteria. Methods Enzymol. 309 (1999) 48-58
12. Goldberg M.E., Rudolph R., and Jaenicke R. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 30 (1991) 2790-2797
13. Gough J.D., Barrett E.J., Silva Y., and Lees W.J. Ortho- and meta-substituted aromatic thiols are efficient redox buffers that increase the folding rate of a disulfide-containing protein. J. Biotechnol. 125 (2006) 39-47
14. a effects on the folding rate of a disulfide containing protein. Biochemistry 42 (2003) 11787-11797
15. a, and thiol concentration. J. Biotechnol. 115 (2005) 279-290
16. Gough J.D., and Lees W.J. Increased catalytic activity of protein disulfide isomerase using aromatic thiol based redox buffers. Bioorg. Med. Chem. Lett. 15 (2005) 777-781
17. Gough J.D., Williams Jr. R.H., Donofrio A.E., and Lees W.J. Folding disulfide-containing proteins faster with an aromatic thiol. J. Am. Chem. Soc. 124 (2002) 3885-3892
18. Gurbhele-Tupkar M.C., Perez L.R., Silva Y., and Lees W.J. Rate enhancement of the oxidative folding of lysozyme by the use of aromatic thiol containing redox buffers. Bioorg. Med. Chem. 16 (2008) 2579-2590
19. Hevehan D.L., and De Bernardez Clark E. Oxidative renaturation of lysozyme at high concentrations. Biotechnol. Bioeng. 54 (1997) 221-230
20. Hillson D.A., Lambert N., and Freedman R.B. Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase. Methods Enzymol. 107 (1984) 281-294
21. Jolles P. Lysozymes from rabbit spleen and dog spleen. Method Enzymol. 5 (1962) 137-140
22. Jungbauer A., and Kaar W. Current status of technical protein refolding. J. Biotechnol. 128 (2007) 587-596
23. Kibria F.M., and Lees W.J. Balancing conformational and oxidative kinetic traps during the folding of bovine pancreatic trypsin inhibitor (Bpti) with glutathione and glutathione disulfide. J. Am. Chem. Soc. 130 (2008) 796-797
24. Kiefhaber T., Rudolph R., Kohler H.H., and Buchner J. Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Bio/Technology 9 (1991) 825-829
25. Konishi Y., Ooi T., and Scheraga H.A. Regeneration of ribonuclease a from the reduced protein. Isolation and identification of intermediates and equilibrium treatment. Biochemistry 20 (1981) 3945-3955
26. Konishi Y., Ooi T., and Scheraga H.A. Regeneration of ribonuclease a from the reduced protein. 1. Rate-limiting steps. Biochemistry 21 (1982) 4734-4740
27. Konishi Y., Ooi T., and Scheraga H.A. Regeneration of ribonuclease a from the reduced protein. 2. Energetic analysis. Biochemistry 21 (1982) 4741-4748
28. Lees W.J. Small-molecule catalysts of oxidative protein folding. Curr. Opin. Chem. Biol. 12 (2008) 740-745
29. Lilie H., Schwarz E., and Rudolph R. Advances in refolding of proteins produced in E. Coli. Curr. Opin. Biotechnol. 9 (1998) 497-501
30. Maeda Y., Yamada H., Ueda T., and Imoto T. Effect of additives on the renaturation of reduced lysozyme in the presence of 4m urea. Protein Eng. 9 (1996) 461-465
31. Mitraki A., and King J. Protein folding intermediates and inclusion body formation. Bio/Technology 7 (1989) 690-697
32. Narayan M., Welker E., Wedemeyer W.J., and Scheraga H.A. Oxidative folding of proteins. Acc. Chem. Res. 33 (2000) 805-812
33. Orsini G., and Goldberg M.E. The renaturation of reduced chymotrypsinogen a in guanidine hydrochloride. Refolding versus aggregation. J. Biol. Chem. 253 (1978) 3453-3458
34. Patil G., Rudolph R., and Lange C. In vitro-refolding of a single-chain Fv fragment in the presence of heteroaromatic thiols. J. Biotechnol. 134 (2008) 218-221
35. Perraudin J.P., Torchia T.E., and Wetlaufer D.B. Multiple parameter kinetic studies of the oxidative folding of reduced lysozyme. J. Biol. Chem. 258 (1983) 11834-11839
36. Rariy R.V., and Klibanov A.M. Correct protein folding in glycerol. Proc. Natl. Acad. Sci. 94 (1997) 13520-13523
37. Reddy K R.C., Lilie H., Rudolph R., and Lange C. l-Arginine increases the solubility of unfolded species of hen egg white lysozyme. Protein Sci. 14 (2005) 929-935
38. Roux P., Delepierre M., Goldberg M.E., and Chaffotte A.F. Kinetics of secondary structure recovery during the refolding of reduced hen egg white lysozyme. J. Biol. Chem. 272 (1997) 24843-24849
39. Rudolph R., and Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10 (1996) 49-56
40. Sahdev S., Khattar S.K., and Saini K.S. Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies. Mol. Cell. Biochem. 307 (2008) 249-264
41. Saxena V.P., and Wetlaufer D.B. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 9 (1970) 5015-5023
42. Szajewski R.P., and Whitesides G.M. Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione. J. Am. Chem. Soc. 102 (1980) 2011-2026
43. Weissman J.S., and Kim P.S. Reexamination of the folding of Bpti: predominance of native intermediates. Science 253 (1991) 1386-1393
44. Weissman J.S., and Kim P.S. Efficient catalysis of disulfide bond rearrangements by protein disulfide isomerase. Nature 365 (1993) 185-188
45. Wetlaufer D.B., and Saxena V.P. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 9 (1970) 5015-5023
46. Wetzel R. Mutations and off-pathway aggregation of proteins. Trends Biotechnol. 12 (1994) 193-198
47. Willis M.S., Hogan J.K., Prabhakar P., Liu X., Tsai K., Wei Y., and Fox T. Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactions. Protein Sci. 14 (2005) 1818-1826
48. Wilson J.M., Bayer R.J., and Hupe D.J. Structure-reactivity correlations for the thiol-disulfide interchange reaction. J. Am. Chem. Soc. 99 (1977) 7922-7926
49. Winter J., Lilie H., and Rudolph R. Recombinant expression and in vitro folding of proinsulin are stimulated by the synthetic dithiol vectrase-P. FEMS Microbiol. Lett. 213 (2002) 225-230
50. Woycechowsky K.J., Hook B.A., and Raines R.T. Catalysis of protein folding by an immobilized small-molecule dithiol. Biotechnol. Prog. 19 (2003) 1307-1314
51. Woycechowsky K.J., and Raines R.T. The Cxc motif: a functional mimic of protein disulfide isomerase. Biochemistry 42 (2003) 5387-5394
52. Woycechowsky K.J., Wittrup K.D., and Raines R.T. A small-molecule catalyst of protein folding in vitro and in vivo. Chem. Biol. 6 (1999) 871-879
53. Zettlmeissl G., Rudolph R., and Jaenicke R. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry 18 (1979) 5567-5571