Role of arginine in the stabilization of proteins against aggregation

Biochemistry

Volumn 44, Issue 12, 2005, Pages 4919-4925

  Baynes, Brian M ^a   Wang, Daniel I C ^a   Trout, Bernhardt L ^a  

^a Massachusetts Institute of Technology Cambridge   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; AGGREGATES; PROTEINS; SOLUTIONS; WATER;

AMINO ACID ARGININE; PROTEIN REFOLDING; PROTEIN-PROTEIN ENCOUNTERS; SOLUTION ADDITIVES;

AMINO ACIDS;

ARGININE; CARBONATE DEHYDRATASE; GLOBULAR PROTEIN; INSULIN; INSULIN ANTIBODY; MONOCLONAL ANTIBODY; PROTEIN; WATER;

ARTICLE; DISSOCIATION; ENERGY; EXPERIMENT; HYPOTHESIS; MOLECULE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; THEORETICAL STUDY;

ANIMALS; ANTIBODIES, MONOCLONAL; ARGININE; CARBONIC ANHYDRASES; CATTLE; DIPEPTIDES; GUANIDINE; HUMANS; INSULIN; INSULIN ANTIBODIES; KINETICS; MODELS, CHEMICAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; SODIUM CHLORIDE; SOLUTIONS; THERMODYNAMICS;

EID: 15444374846     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047528r     Document Type: Article

References (41)

1. Lilie, H., Schwarz, E., and Rudolph, R. (1998) Advances in refolding of proteins produced in E. coli, Curr. Opin. Biotechnol. 9, 497-501.
2. Dill, K. A. (1990) Dominant forces in protein folding, Biochemistry 29, 7133-7155.
3. Zettlmeissl, G., Rudolph, R., and Jaenicke, R. (1979) Reconstitution of lactic dehydrogenase. noncovalent aggregation vs. reactivation. 1. physical properties and kinetics of aggregation, Biochemistry 18, 5567-5571.
4. Wang, W. (1999) Instability, stabilization, and formulation of liquid protein pharmaceuticals, Int. J. Pharmacol. 185, 129-188.
5. Cleland, J. L., Powell, M. F., and Shire, S. J. (1993) The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation, Crit. Rev. Ther. Drug Carrier Syst. 10, 307-377.
6. Arakawa, T., and Tsumoto, K. (2003) The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation, Biochem. Biophys. Res. Commun. 304, 148-152.
7. Taneja, S., and Ahmad, F. (1994) Increased thermal stability of proteins in the presence of amino acids, Biochem. J. 303, 147-153.
8. Shiraki, K., Kudou, M., Fujiwara, S., Imanaka, T., and Takagi, M. (2002) Biophysical effect of amino acids on the prevention of protein aggregation, J. Biochem. 132, 591-595.
9. Rudolph, R., Fischer, S., and Mattes, R. (1985) Patent DE3537708, Process for the Activation of tPA after Expression in Prokaryotic Cells.
10. Arora, D., and Khanna, N. (1996) Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies, J. Biotechnol. 52, 127-133.
11. Armstrong, N., de Lencastre, A., and Gouaux, E. (1999) A new protein folding screen: Application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase, Protein Sci. 8, 1475-1483.
12. Rinas, U., Risse, B., Jaenicke, R., Abel, K.-J., and Zettlmeissl, G. (1990) Denaturation-renaturation of the fibrin-stabilizing factor xiii a-chain isolated from human placenta, Biol. Chem. Hoppe-Seyler 371, 49-56.
13. Buchner, J., and Rudolph, R. (1991) Renaturation, purification and characterization of recombinant fab-fragments produced in Escherichia coli, Biotechnology 9, 157-162.
14. Tsumoto, K., Umetsu, M., Kumagai, I., Ejima, D., Philo, J. S., and Arakawa, T. (2004) Role of arginine in protein refolding, solubilization, and purification, Biotechnol. Prog. 20, 1301-1308.
15. Baynes, B. M., and Trout, B. L. (2004) Rational design of solution additives for the preventing of protein aggregation, Biophys. J. 87, 1631-1639.
16. Baynes, B. M., and Trout, B. L. (2003) Proteins in mixed solvents: A molecular-level perspective, J. Phys. Chem. B 107, 14058-14067.
17. Timasheff, S. N. (1998) Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated, Adv. Protein Chem. 51, 355-431.
18. Colombo, M. F., Rau, D. C., and Parsegian, A. (1992) Protein solvation in allosteric regulation: A water effect on hemoglobin, Science 256, 655-659.
19. Kirkwood, J. G., and Buff, F. P. (1951) The statistical mechanical theory of solutions, i, J. Ghent Phys. 19, 774-777.
20. Shimizu, S. (2004) Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments, Proc. Natl. Acad. Sci. U.S.A. 101, 1195-1199.
21. Shimizu, S., and Smith, D. J. (2004) Preferential hydration and the exclusion of cosolvents from protein surfaces, J. Chem. Phys. 121, 1148-1154.
22. Smith, P. E. (2004) Local chemical potential equalization model for cosolvent effects on biomolecular equilibria, J. Phys. Chem. B 108, 16271-16278.
23. Minton, A. P. (1997) Influence of excluded volume upon macromolecular structure and associations in crowded media, Curr. Opin. Biotechnol. 8, 65-69.
24. Linder, R., and Ralston, G. (1995) Effects of dextran on the self-association of human spectrin, Biophys. Chem. 57, 15-25.
25. Pocker, Y., and Stone, J. T. (1967) The catalytic versatility of erythrocyte carbonic anhydrase. iii. kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate, Biochemistry 6, 668-678.
26. Pocker, Y., and Biswas, S. B. (1981) Self-association of insulin and the role of hydrophobic bonding: A thermodynamic model of insulin dimerization, Biochemistry 20, 4354-4361,
27. Cleland, J. L., Hedgepeth, C., and Wang, D. I. C. (1992) Polyethylene glycol enhanced refolding of bovine carbonic anhydrase b, J. Biol. Chem. 267, 13327-13334.
28. Wetlaufer, D. B., and Xie, Y. (1995) Control of aggregation in protein refolding: A variety of surfactants promote renaturation of carbonic anhydrase ii, Protein Sci. 4, 1535-1543.
29. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding, Protein Sci. 4, 2138-2148.
30. Lee, J. C., and Timasheff, S. N. (1974) Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride, Biochemistry 13, 257-265.
31. Gekko, K., and Timasheff, S. N. (1981) Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures, Biochemistry 20, 4667-4676.
32. Arakawa, T., and Timasheff, S. N. (1985) The stabilization of proteins by osmolytes, Biophys. J. 47, 411-414.
33. Timasheff, S. N. (2002) Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components, Proc. Natl. Acad. Sci. U.S.A. 99, 9721-9726.
34. Davis-Searles, P. R., Saunders, A. J., Erie, D. A., Winzor, D. J., and Pielak, G. J. (2001) Interpreting the effects of small uncharged solutes on protein-folding equilibria, Annu. Rev. Biophys. Biomol. Struct. 30, 271-306.
35. Semisotnov, G., Rodionova, N. A., Kutyshenko, V. P., Ebert, B., Blanck, J., and Ptitsyn, O. B. (1987) Sequential mechanism of refolding of carbonic anhydrase b, FEBS Lett. 224, 9-13.
36. Semisotnov, G. V., Uversky, V. N., Sokolovsky, I. V., Gutin, A. M., Razgulyaev, O. I., and Rodionova, N. A. (1990) 2 slow stages in refolding of bovine carbonic anhydrase-b are due to proline isomerization, J. Mol. Biol. 213, 561-568.
37. Dolgikh, D. A., Kolomiets, A. P., Bolotina, I. A., and Ptitsyn, O. B. (1984) Molten-globule state accumulates in carbonic anhydrase folding, FEBS Lett. 165, 88-92.
38. Cleland, J. L. (1991) Mechanisms of Protein Aggregation and Refolding, Ph.D. Thesis, Massachusetts Institute of Technology, Cambridge.
39. Cleland, J. L., and Wang, D. I. C. (1992) Transient association of the first intermediate during the refolding of bovine carbonic anhydrase b, Biotechnol. Prog. 6, 97-103.
40. Cleland, J. L., and Wang, D. I. C. (1990) Refolding and aggregation of bovine carbonic anhydrase b: Quasi-elastic light scattering analysis, Biochemistry 29, 11072-11078.
41. Hevehan, D. L., and Clark, E. D. B. (1997) Oxidative renaturation of lysozyme at high concentrations, Biotechnol. Bioeng. 54, 221-230.