Thermal dissociation and unfolding of insulin

Biochemistry

Volumn 44, Issue 33, 2005, Pages 11171-11177

  Huus, Kasper ^a   Havelund, Svend ^b   Olsen, Helle B ^b   Van De Weert, Marco ^a   Frokjaer, Sven ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b NOVO NORDISK A S   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

APPROXIMATION THEORY; DIFFERENTIAL SCANNING CALORIMETRY; DISSOCIATION; ENTHALPY; HIGH TEMPERATURE EFFECTS; IONS; MONOMERS; OLIGOMERS; PROTEINS; THERMODYNAMIC STABILITY; ULTRAVIOLET RADIATION;

CIRCULAR DICHROISM; HEXAMERS; MUTANTS; THERMAL DENATURATION PATTERN;

INSULIN;

ASPARTIC ACID; DIMER; GLUTAMIC ACID; HUMAN INSULIN; INSULIN; MONOMER; MUTANT PROTEIN; OLIGOMER; ZINC;

ARTICLE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; DISSOCIATION; ENTHALPY; HEATING; HORMONE STRUCTURE; HUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; ROOM TEMPERATURE; TEMPERATURE DEPENDENCE; THERMAL EXPOSURE; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; HEAT; HUMANS; INSULIN; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; ZINC;

EID: 23944504732     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0507940     Document Type: Article

References (38)

1. Blundell, T. L. (1972) Three-dimensional atomic structure of insulin and its relationship to activity, Diabetes 21, 492-505.
2. Grant, P. T., Coombs, T. L., and Frank, B. H. (1972) Differences in the nature of the interaction of insulin and proinsulin with zinc, Biochem. J. 126, 433-440.
3. Goldman, J., and Carpenter, F. H. (1974) Zinc binding, circular dichroism, and equilibrium sedimentation studies on insulin (bovine) and several of its derivatives, Biochemistry 13, 4566-4574.
4. Summerell, J. M., Osmand, A., and Smith, G. H. (1965) An equilibrium-dialysis study of binding of zinc to insulin, Biochem. J. 95, 31.
5. Emdin, S. O., Dodson, G. G., Cutfield, J. M., and Cutfield, S. M. (1980) Role of zinc in insulin biosynthesis. Some possible zinc-insulin interactions in the pancreatic B-cell, Diabetologia 19, 174-182.
6. Kaarsholm, N. C., Ko, H. C., and Dunn, M. F. (1989) Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin, Biochemistry 28, 4427-4435.
7. Brange, J. (1994), Stability of insulin: Studies on the physical and chemical stability of insulin in pharmaceutical formulation. Thesis (Dr. Pharm.), Kluwer Academic Publishers, Dordrecht, The Netherlands.
8. Banting, F. G., and Best, C. H. (1922) The internal secretion of the pancreas, J. Lab. Clin. Med. 7, 251-266.
9. Banting, F. G., Best, C. H., Collip, J. B., and Macleod, J. J. R. (1922) The preparation of pancreatic extracts containing insulin, Trans. R. Soc. Chem. 16, 27-29.
10. Bouchard, M., Zurdo, J., Nettleton, E. J., Dobson, C. M., and Robinson, C. V. (2000) Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9, 1960-1967.
11. Hua, Q. X., and Weiss, M. A. (2004) Mechanism of Insulin Fibrillation: The structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate, J. Biol. Chem. 279, 21449-21460.
12. Ettinger, M. J., and Timasheff, S. N. (1971) Optical activity of insulin. I. On the nature of the circular dichroism bands, Biochemisty 10, 824-831.
13. Volkin, D. B., and Klibanov, A. M. (1987) Thermal destruction processes in proteins involving cystine residues, J. Biol. Chem. 262, 2945-2950.
14. Dzwolak, W., Ravindra, R., Lendermann, J., and Winter, R. (2003) Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy, Biochemistry 42, 11347-11355.
15. Nielsen, L., Frokjaer, S., Brange, J., Uversky, V. N., and Fink, A. L. (2001) Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry 40, 8397-8409.
16. Cooper, A. (2005) Heat capacity effects in protein folding and ligand binding: A re-evaluation of the role of water in biomolecular thermodynamics. Biophys. Chem. 115, 89-97.
17. Brange, J., Langkjaer, L., Havelund, S., and Volund, A. (1992) Chemical stability of insulin. 1. Hydrolytic degradation during storage of pharmaceutical preparations, Pharm. Res. 9, 715-726.
18. Brange, J., Havelund, S., and Hougaard, P. (1992) Chemical stability of insulin. 2. Formation of higher molecular weight transformation products during storage of pharmaceutical preparations, Pharm. Res. 9, 727-734.
19. Brange, J. (1992) Chemical stability of insulin. 5. Isolation, characterization and identification of insulin transformation products, Acta Pharm. Nord 1992 (4), 223-232.
20. Brange, J., Ribel, U., Hansen, J. F., Dodson, G., Hansen, M. T., Havelund, S., Melberg, S. G., Morris, F., Norris, K., Snel, L., Soørensen, A. R., and Voigt, H. O. (1988) Monomeric insulins obtained by protein engineering and their medical implications. Nature 333, 679-682.
21. Plotnikov, V. V., Brandts, J. M., Lin, L. N., and Brandts, J. F. (1997) A new ultrasensitive scanning calorimeter, Anal. Biochem. 250, 237-244.
22. Grek, S. B., Davis, J. K., and Blaber, M. (2001) An efficient, flexible-model program for the analysis of differential scanning calorimetry protein denaturation data, Protein Pept. Lett. 6, 429-436.
23. Strickland, E. H., and Mercola, D. (1976) Near-ultraviolet tyrosyl circular dichroism of pig insulin monomers, dimers, and hexamers. Dipole-dipole coupling calculations in the monopole approximation, Biochemistry 15, 3875-3884.
24. Ahmad, A., Millett, I. S., Doniach, S., Uversky, V. N., and Fink, A. L. (2003) Partially folded intermediates in insulin fibrillation. Biochemistry 42, 11404-11416.
25. Bryant, C., Strohl, M., Green, L. K., Long, H. B., Alter, L. A., Pekar, A. H., Chance, R. E., and Brems, D. N. (1992) Detection of an equilibrium intermediate in the folding of a monomeric insulin analog, Biochemistry 31, 5692-5698.
26. Nielsen, L., Khurana, R., Coats, A., Frokjaer, S., Brange, J., Vyas, S., Uversky, V. N., and Fink, A. L. (2001) Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism, Biochemistry 40, 6036-6046.
27. Millican, R. L., and Brems, D. N. (1994) Equilibrium intermediates in the denaturation of human insulin and two monomeric insulin analogs, Biochemistry 33, 1116-1124.
28. Kaarsholm, N. C., Morris, K., Jorgensen, R. J., Mikkelsen, J., Ludvigsen, S., Olsen, O. H., Sorensen, A. R., and Havelund, S. (1993) Engineering stability of the insulin monomer fold with application to structure-activity relationships, Biochemistry 32, 10773-10778.
29. Hansen, J. F. (1991) The self-association of zinc-free human insulin and insulin analogue B13-glutamine, Biophys. Chem. 39, 107-110.
30. Shrake, A., and Ross, P. D. (1988) Biphasic denaturation of human albumin due to ligand redistribution during unfolding, J. Biol. Chem. 263, 15392-15399.
31. Brandts, J. F., and Lin, L. N. (1990) Study of strong to ultralight protein interactions using differential scanning calorimetry. Biochemistry 29, 6927-6940.
32. Barone, G., Delvecchio, P., Fessas, D., Giancola, C., Graziano, G., and Riccio, A. (1994) Ligand-induced biphasic thermaldenaturation of RNAase A, J. Therm. Anal. 41, 1263-1276.
33. Wasylewski, M. (2004) Evaluation of riboflavin binding protein domain interaction using differential scanning calorimetry, Biochim. Biophys. Acta 1702, 137-143.
34. Shrake, A., and Ross, P. D. (1992) Origins and consequences of ligand-induced multiphasic thermal protein denaturation, Biopolymers 32, 925-940.
35. Robert, C. H., Gill, S. J., and Wyman, J. (1988) Quantitative analysis of linkage in macromolecules when one ligand is present in limited total quantity, Biochemistry 27, 6829-6835.
36. Ahmad, A., Millett, I. S., Doniach, S., Uversky, V. N., and Fink, A. L. (2004) Stimulation of insulin fibrillation by urea-induced intermediates, J. Biol. Chem. 279, 14999-15013.
37. 1H nuclear magnetic resonance study of the histidine residues of insulin, J. Mol. Biol. 150, 609-613.
38. Adams, M. J. (1969) Structure of rhombohedral 2 Zn insulin crystals, Nature 224, 491-495.