Theoretic information approach to protein stabilization by solvent engineering

AIChE Journal

Volumn 46, Issue 7, 2000, Pages 1478-1489

  Di Domenico, Roberto ^a   Lavecchia, Roberto ^a   Ottavi, Alessandro ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ADDITIVES; BINARY MIXTURES; COMPUTER SIMULATION; CONFORMATIONS; HYDROGEN BONDS; MOLECULAR DYNAMICS; MOLECULAR ORIENTATION; MOLECULAR STRUCTURE; SOLVENTS; THERMODYNAMICS; VAN DER WAALS FORCES;

MOLECULAR THERMODYNAMICS; PROTEIN STABILIZATION; SOLVENT EFFECT;

PROTEINS;

SOLVENT;

ARTICLE; CALCULATION; ENERGY TRANSFER; GENETIC ENGINEERING; INFORMATION SCIENCE; MODEL; PROTEIN CONFORMATION; PROTEIN STABILITY; THERMODYNAMICS;

EID: 0034233776     PISSN: 00011541     EISSN: None     Source Type: Journal    
DOI: 10.1002/aic.690460721     Document Type: Article

References (63)

1. Arakawa, T., and S. N. Timasheff, "Stabilization of Protein Structure by Sugars," Biochemistry, 21, 6536 (1982).
2. Arakawa, T., and S. N. Timasheff, "Preferential Interactions of Proteins with Solvent Components in Aqueous Amino Acid Solutions," Arch. Biochem. Biophys., 224. 169 (1983).
3. Arakawa, T., R. Bhat, and S. N. Timasheff, "Why Preferential Hydration does not Always Stabilize the Native Structure of Globular Proteins," Biochemistry, 29, 1924 (1990).
4. Asenjo, J. A., and I. Patrick, "Large-Scale Protein Purification," Protein Purification Application. A Practical Approach, E. L. V. Harris and S: Angal, eds., IRL Press, Oxford, p. 1 (1990).
5. Becktel, W. J., and J. A. Schellman, "Protein Stability Curves," Biopolymers, 26, 1859 (1987).
6. Bhat, R., and S. N. Timasheff, "Steric Exclusion Is the Principal, Source of the Preferential Hydration of Proteins in the Presence of Polyethylene Glycols," Protein Sci., 1, 1133 (1992).
7. Blake, C. C. F., D. E. P. Grace, L. N. Johnson, S. J. Perkins, D. C. Philips, R. Cassels, C. M. Dobson, F. M. Poulsen, and R. J. P. Williams, "Physical and Chemical Properties of Lysozyme," Molecular Interactions and Activity in Proteins, Excerpta Medica, Amsterdam, p. 137 (1978).
8. Bonchev, D., Information Theoretic Indices for Characterization of Chemical Structures, Wiley, New York (1983).
9. Bonchev, D., and N. Trinajstic, "Information Theory, Distance Matrix and Molecular Branching," J. Chem. Phys., 67, 4517 (1977).
10. Bonchev, D., and N. Trinajstic, "On Topological Characterization of Molecular Branching," Int. J. Quant. Chem., 12, 293 (1978).
11. Cioci, F., "Thermostabilization of Erthyrocyte Carbonic Anhydrase by Polyhydric Addtiives," Enzyme Microb. Technol., 17, 592 (1995a).
12. Cioci. F., "Catalytic Activity of Aspergillus Niger Glucose Oxidase in Water-Polyol Mixtures," Catal. Lett., 35, 395 (1995b).
13. Cioci, F., and R. Lavecchia, "Effect of Polyols and Sugars on Heat-Induced Flavin Dissociation in Glucose Oxidase," Biochem. Mol. Biol. Int., 34, 705 (1994).
14. Cioci, F., and R. Lavecchia, "Molecular Thermodynamics of Heat-Induced Protein Unfolding in Aqueous Media," AIChE J., 43, 525 (1997a).
15. Cioci, F., and R. Lavecchia, "Interfacial Phenomena and Solvent Effects in Protein Stability," Rec. Res. Dev. Phys. Chem., 1, 369 (1997b).
16. Cioci, F., and R. Lavecchia, "Thermostabilization of Proteins by Water-Miscible Additives," Chem. Biochem. Eng. Q., 12, 191 (1998).
17. Cioci, F., and R. Lavecchia, "Sorbitol-Mediated Stabilization of Human IgG Against Thermal Inactivation," Biotech. Tech., (1999).
18. Cioei, F., R. Lavecchia, and L. Marrelli, "Perturbation of Surface Tension of Water by Polyhydric Additives: Effect on Glucose Oxidase Stability," Biocatalysis, 10, 137 (1994).
19. Cioci, F., R. Lavecchia, and L. Marrelli, "Effect of Surface Tension on the Conformational Stability of Erthyrocyte Carbonic Anhydrase," Fluid Phase Equilibria, 116, 118 (1996).
20. Creighton, T. E., "Stability of Folded Conformations," Curr. Opinion Struct. Biol., 1, 5 (1991).
21. Creishton, T. E., Proteins: Structures and Molecular Properties, 2nd ed., Freeman, New York, p. 154 (1993).
22. Dancoff, S. M., and H. Quastler, Essays on the Use of Information Theory in Biology, H. Quastler, ed., Illinois Univ. Press, Urbana (1953).
23. Dill, K. A., "Theory for the Folding and Stability of Globular Proteins," Biochemistry, 24, 1501 (1985).
24. Dill, K. A., "Dominant Forces in Protein Folding," Biochemistry, 29, 7133 (1990).
25. Fernandez, M. M., D. S. Clark, and H. W. Blanch, "Papain Kinetics in the Presence of a Water-Miscible Organic Solvent," Biotech. Bioeng., 37, 967 (1991).
26. Gekko, K., "Calorimetric Study on Thermal Denaturation of Lysozyme in Polyol-Water Mixtures," J. Biochem., 91, 1197 (1982).
27. Greene, R. F., and C. N. Pace "Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, α-Chymotrypsin and β-Lactoglobulin," J. Biol. Chem., 249, 5388 (1974).
28. Kier, L. B., and L. H. Hall, Molecular Connectivity in Chemistry and Drug Research, Academic Press, New York (1976).
29. Klibanov, A. M., "Stabilization of Enzymes Against Thermal Inactivation," Adv. Appl. Microbiol., 29, 1 (1983).
30. Laane, C., S. Boeren, R. Hilhorst, and C. Veeger, "Optimization of Biocatalysis in Organic Media," Biocatalysis in Organic Media, C. Laane, J. Tramper, and M. D. Lilly, eds., Elsevier, Amsterdam, p. 65 (1987).
31. Lavecchia, R., and M. Zugaro, "Thermal Denaturation of Ervthrocyte Carbonic Anhydrase," FEBS Lett., 292, 162 (1991).
32. Lozano, P., D. Combes, and J. L. Iborra, "Effect of Polyols on α-Chymotrypsin Thermostability: A Mechanistic Analysis of the Enzyme Stabilization," J. Biotech., 35, 9 (1994).
33. Matsumoto, M., K. Kida, and K. Kondo, "Effects of Polyols and Organic Solvents on Thermostability of Lipase," J. Chem. Technol. Biotechnol., 70, 188 (1997).
34. Pace, C. N., "The Stability of Globular Proteins," CRC Crit. Rev. Biochem., 3, 1 (1975).
35. Pace, C. N., "Conformational Stability of Globular Proteins," Trends Biochem. Sci., 15, 14 (1990).
36. Pace, C. N., and D. V. Laurents, "A New Method for Determining the Heat Capacity Change for Protein Folding," Biochemistry, 28, 2520 (1989).
37. Pace, C. N., B. A. Shirley, and J. A. Thomson, "Measuring the Conformational Stability of a Protein," Protein Structure: A Practical Approach, T. E. Creighton, ed., IRL Press, Oxford, p. 311 (1989).
38. Pace, C. N., B. A. Shirley, M. McNutt, and K. Gajiwala, "Forces Contributing to the Conformational Stability of Proteins," FASEB J., 10, 75 (1996).
39. Pfeil, W., and P. L. Privalov, "Conformational Changes in Proteins," Biochemical Thermodynamics, M. N. Jones, ed., Elsevier, Amsterdam, p. 75 (1979).
40. Pocker, Y., and S. Sarkanen, "Carbonic Anhydrase: Structure, Catalytic Versatility and Inhibition," Adv. Enzymol., 47, 149 (1978).
41. Privalov, P. L., "Stability of Proteins," Adv. Protein Chem., 33, 167 (1979).
42. Privalov, P. L., and S. J. Gill, "Stability of Protein Structure and Hydrophobic Interaction," Adv. Protein Chem., 39, 191 (1988).
43. Russell, A. J., and C. Vierheller, "Protein Engineering," The Biochemical Engineering Handbook, J. D. Bronzio, ed., CRC Press, New York, p. 1445 (1995).
44. 2 Removal," ASAIO Trans., 36, 486 (1990).
45. Santoro, M. M., and D. W. Bolen, "Unfolding Free Energy Changes Determined by the Linear Extrapolation Method," Biochemistry, 27, 8063 (1988).
46. Santoro, M. M., and D. W. Bolen, "A Test to the Linear Extrapolation of Unfolding Free Energy Changes over an Extended Dcnaturant Concentration Range," Biochemistry, 31, 4901 (1992).
47. Santoro, M. M., Y. Liu, S. M. A. Khan, L. X. Hou, and D. W. Bolen, "Increased Thermal Stability of Proteins in the Presence of Naturally Occurring Osmolytes," Biochemistry, 31, 5278 (1992).
48. Schellman, J. A., "Solvent Denaturation," Biopolymers, 17, 1305 (1978).
49. Schellman, J. A., "Selective Binding and Solvent Denaturation," Biopolymers, 26, 549 (1987).
50. Schellman, J. A., "A Simple Model for Solvation in Mixed Solvents. Application to the Stabilization and Destabilization of Macromolecular Structures," Biophys. Chem., 37, 121 (1990).
51. Schellman, J. A., "The Thermodynamics of Solvent Exchange," Biopolymers, 34, 1015 (1994).
52. Schmid, F. X., "Spectral Methods of Characterizing Protein Conformation and Conformational Changes," Protein Structure: A Practical Approach, T. E. Creighton, ed., IRL Press, Oxford, p. 251 (1989).
53. Shortle, D., A. K. Meeker, and S. L. Gerring, "Effects of Denaturans at Low Concentrations on the Reversible Denaturation of Staphylococcal Nuclease," Arch. Biochem. Biophys., 272, 103 (1989).
54. Squire, P. G., and M. E. Himmel, "Hydrodynamics and Protein Hydration," Arch. Biochem. Biophys., 196, 165 (1979).
55. Tanford, C., "Protein Denaturation. The Transition from Native to Denatured State," Adv. Protein Chem., 23, 121 (1968).
56. Tanford, C., "Protein Denaturation. Theoretical Models for the Mechanism of Denaturation" Adv. Protein Chem., 24, 1 (1970).
57. Thakar, M., A. Bilenko, and W. J. Becktel, "Osmolyte Mediation of T7 DNA Polymerase and Plasmid DNA Stability," Biochemistry, 33, 12255 (1994).
58. Timasheff, S. N., "Water as Ligand: Preferential Binding and Exclusion of Denaturants in Protein Unfolding," Biochemistry, 31, 9857 (1992).
59. Timasheff, S. N., and T. Arakawa, "Stabilization of Protein Structure by Solvents," Protein Structure: A Practical Approach, T. E. Creighton, ed., IRL Press, Oxford, p. 331 (1989).
60. Tomazic, S. J., "Protein Stabilization," Biocatalysis for Industry, J. S. Dordick, ed., Plenum Press, New York, p. 241 (1991).
61. Volkin, D. B., and A. M. Klibanov, "Minimizing Protein Inactivation," Protein Function: A Practical Approach, T. E. Creighton, ed., IRL Press, Oxford, p. 1 (1989).
62. Wilson, R. J., Introduction to Graph Theory, Academic Press, New York (1972).
63. Wyman, J., and S. J. Gill, Binding and Linkage: Functional Chemistry of Biological Macromolecules, Univ. Science Books, Mill Valley, CA (1990).