Temperature-Induced Dissociation of Protein Aggregates: Accessing the Denatured State

Biochemistry

Volumn 42, Issue 48, 2003, Pages 14234-14241

  Meersman, Filip ^a,b   Heremans, Karel ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; DISSOCIATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PROTEINS;

NONREDUCING CONDITIONS;

BIOCHEMISTRY;

DEUTERIUM; HYDROGEN; LYSOZYME; PANCREATIC RIBONUCLEASE; REDUCING AGENT; RIBONUCLEASE A;

ANIMAL; ARTICLE; CATTLE; CHEMICAL BOND; CHEMISTRY; CHICKEN; COLD; COMPARATIVE STUDY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COOLING; CORRELATION ANALYSIS; DEUTERIUM HYDROGEN EXCHANGE; DISSOCIATION; ENZYME ANALYSIS; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; HEAT; HEATING; INFRARED SPECTROSCOPY; LOW TEMPERATURE; MACROMOLECULE; NONHUMAN; OXIDATION REDUCTION REACTION; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; PROTON TRANSPORT; REDUCTION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

ANIMALS; CATTLE; CHICKENS; COLD; DEUTERIUM EXCHANGE MEASUREMENT; ENZYME STABILITY; HEAT; MACROMOLECULAR SUBSTANCES; MURAMIDASE; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN DENATURATION; RIBONUCLEASE, PANCREATIC; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS;

ANIMALIA; BOS TAURUS; GALLUS GALLUS;

EID: 0344198173     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035623e     Document Type: Article

References (56)

1. De Young, L. R., Dill, K. A., and Fink, A. L. (1993) Aggregation and denaturation of apomyoglobin in aqueous urea solutions, Biochemistry 32, 3877-3886.
2. Fink, A. L. (1998) Protein aggregation: folding aggregates, inclusion bodies and amyloid, Fold. Des. 3, R9-R23.
3. Dobson, C. M. (2001) The structural basis of protein folding and its links with human disease, Philos. Trans. R. Soc. London B 356, 133-145.
4. Holzbaur, I. E., English, A. M., and Ismail, A. A. (1996) FTIR study of the thermal denaturation of horseradish and cytochrome c peroxidases in D20, Biochemistry 35, 5488-5495.
5. Litvinovich, S. V., Brew, S. A., Aota, S., Akiyama, S. K., Haudenschild, C., and Ingham, K. C. (1998) Formation of amyloid-like fibrils by self-association of a partially folded fibronectin type III module, J. Mol. Biol. 280, 245-258.
6. Dubois, J., Ismail, A. A., Chan, S. L., and Ali-Khan, Z. (1999) Fourier transform infrared spectroscopic investigation of temperature- and pressure-induced disaggregation of amyloid A, Scand. J. Immunol. 49, 376-380.
7. West, M. W., Wang, W. X., Patterson, J., Mancias, J. D., Beasley J. R., and Hecht, M. H. (1999) De novo amyloid proteins from designed combinatorial libraries, Proc. Natl. Acad. Sci. U.S.A. 96, 11211-11216.
8. Koscielska-Kasprzak, K., and Otlewski, J. (2003) Amyloid-forming peptides selected proteolytically from phage display library, Protein Sci. 12, 1675-1685.
9. Silva, J. L., and Weber, G. (1993) Pressure stability of proteins, Annu. Rev. Phys. Chem. 44, 89-113.
10. Gorovits, B. M., and Horowitz, P. M. (1998) High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure, Biochemistry 37, 6132-6135.
11. Smeller, L., Rubens, P., and Heremans, K. (1999) Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin, Biochemistry 38, 3816-3820.
12. Foguel, D., Robinson, C. R., Caetano de Sousa, P., Jr., Silva, J. L., and Robinson, A. S. (1999) Hydrostatic pressure rescues native protein from aggregates, Biotechnol. Bioeng. 63, 552-558.
13. St. John, R. J., Carpenter, J. F., Balny, C., and Randolph, T. W. (2001) High-pressure refolding of recombinant human growth hormone from insoluble aggregates, J. Biol Chem. 276, 46856-46863.
14. Parsell, D. A., Kowal, A. S., Singer, M. A., and Lindquist, S. (1994) Protein disaggregation mediated by heat-shock protein Hsp104, Nature 372, 475-478.
15. Solomon, B., Koppel, R., Frankel, D., and Hanan-Aharon, E. (1997) Disaggregation of Alzheimer β-amyloid by site-directed mAb, Proc. Natl. Acad. Sci. U.S.A. 94, 4109-4112.
16. Ismail, A. A., Mantsch, H. H., and Wong, P. T. T. (1992) Aggregation of chymotrypsin: portrait by infrared spectroscopy, Biochim. Biophys. Acta 1121, 183-188.
17. Damaschun, G., Damaschun, H., Fabian, H., Gast, K., Krober, R., Wieske, M., and Zirwer, D. (2000) Conversion of yeast phosphoglycerate kinase into amyloid-like structure, Proteins 39, 204-211.
18. Dong, A., Randolph, T. W., and Carpenter, J. F. (2000) Entrapping intermediates of thermal aggregation in α-helical proteins with low concentration of guanidine hydrochloride, J. Biol Chem. 275, 27689-27693.
19. van Stokkum, I. H. M., Linsdell, H., Hadden, J. M., Haris, P. I., Chapman, D., and Bloemendal, M. (1995) Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis, Biochemistry 34, 10508-10518.
20. Fabian, H., Schultz, C., Naumann, D., Landt, O., Hahn, U., and Saenger, W. (1993) Secondary structure and temperature-induced unfolding and refolding of ribonuclease TI in aqueous solution. A Fourier transform infrared spectroscopic study, J. Mol. Biol. 232, 967-981.
21. Torrent, J., Rubens, P., Ribo, M., Heremans, K., and Vilanova, M. (2001) Pressure versus temperature unfolding of ribonuclease A: an FTIR spectroscopic characterization of 10 variants at the carboxy-terminal site, Protein Sci. 10, 725-734.
22. Panick, G., and Winter, R. (2000) Pressure-induced unfolding/ refolding of ribonuclease A: static and kinetic Fourier transform infrared spectroscopy study, Biochemistry 39, 1862-1869.
23. Smeller, L., Goossens, K., and Heremans, K. (1995) How to minimize certain artifacts in Fourier self-deconvolution, Appl. Spectrosc. 49, 1538-1542.
24. Byler, D. M., and Susi, H. (1986) Examination of the secondary structure of proteins by deconvolved FTIR spectra, Biopolymers 25, 469-487.
25. Smeller, L., Goossens, K., and Heremans, K. (1995) Determination of the secondary structure of proteins at high pressure, Vibr. Spectrosc. 8, 199-203.
26. Press, W. H., Flannery, B. P., Teukolsky, S. A., and Vetterling, W. T. (1986) In Numerical recipes: the art of scientific computing, Cambridge University Press, Cambridge, U.K., Chapter 12.6.
27. Fabian, H., Mantsch, H. H., and Schultz, C. P. (1999) Two-dimensional IR correlation spectroscopy: Sequential events in the unfolding process of the λ Cro-V55C repressor protein, Proc. Natl. Acad. Sci. U.S.A. 96, 13153-13158.
28. Dzwolak, W., Kato, M., Shimizu, A., and Taniguchi, Y. (2000) Comparative two-dimensional Fourier transform infrared correlation spectroscopic study on the spontaneous, pressure-, and temperature-enhanced H/D exchange in α-lactalbumin, Appl. Spectrosc. 54, 963-967.
29. Jackson, M., and Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
30. 10-helices in globular proteins, Int. J. Pept. Protein Res. 37, 508-512.
31. Goldberg, M. E., Rudolph, R., and Jaenicke, R. (1991) A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme, Biochemistry 30, 2790-2797.
32. Paquet, M.-J., Laviolette, M., Pézolet, M., and Auger, M. (2001) Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol, Biophys. J. 81, 305-312.
33. Wedemeyer, W. J., Welker, E., Narayan, M., and Scheraga, H. A. (2000) Disulfide bonds and protein folding, Biochemistry 39, 4207-4216.
34. Englander, S. W., Mayne, L., Bai, Y., and Sosnick, T. R. (1997) Hydrogen exchange: The modern legacy of Linderstrom-Lang, Protein Sci. 6, 1101-1109.
35. Radford, S, E., Buck, M., Topping, K. D., Dobson, C. M., and Evans, P. A. (1991) Hydrogen exchange in native and denatured states of hen egg-white lysozyme, Proteins: Struct., Funct., Genet. 14, 237-248.
36. Matagne, A., Jamin, M., Chung, E. W., Robinson, C. V., Radford, S. E., and Dobson, C. M. (2000) Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme, J. Mol. Biol. 297, 193-210.
37. Mark, A. E., and Van Gunsteren, W. F. (1992) Simulation of the thermal denaturation of hen egg white lysozyme: trapping the molten globule state, Biochemistry 31, 7745-7748.
38. Rahmelow, K, Hübner, W., and Ackermann, Th. (1998) Infrared absorbances of protein side chains, Anal. Biochem. 257, 1-11.
39. van den Berg, B., Ellis, R. J., and Dobson, C. M. (1999) Effects of macromolecular crowding on protein folding and aggregation, EMBO J. 18, 6927-6933.
40. Morozova-Roche, L. A., Zurdo, J., Spencer, A., Noppe, W., Receveur, V., Archer, D. B., Joniau, M., and Dobson, C. M. (2000) Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants, J. Struct. Biol. 130, 339-351.
41. Booth, D. R., Sunde, M., Bellotti, V., Robinson, C. V., Hutchinson, W. L., Fraser, P. E., Hawkins, P. N., Dobson, C. M., Radford, S. E., Blake, C. C. F., and Pepys, M. B. (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis, Nature 385, 787-793.
42. Balbimie, M., Grothe, R., and Eisenberg, D. S. (2001) An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid, Proc. Natl. Acad. Sci. U.S.A. 98, 2375-2380.
43. Chamberlain, A. K., Receveur, V., Spencer, A., Redfield, C., and Dobson, C. M. (2001) Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy, Protein Sci. 10, 2525-2530.
44. Denisov, V. P., and Halle, B. (1998) Thermal denaturation of ribonuclease A characterized by water 0-17 and H-2 magnetic relaxation dispersion, Biochemistry 37, 9595-9604.
45. Hagihara, Y., Hoshino, M., Hamada, D., Kataoka, M., and Goto, Y. (1998) Chainlike conformation of heat-denatured ribonuclease A and cytochrome c as evidenced by solution X-ray scattering, Fold. Des. 3, 195-201.
46. Navon, A., Ittah, V., Laity, J. H., Scheraga, H. A., Haas, E., and Gussakovsky, E. E. (2001) Local and long-range interactions in the thermal unfolding transition of bovine pancreatic ribonuclease A, Biochemistry 40, 93-104.
47. Klink, T. A., Woycechowsky, K. J., Taylor, T. M., and Raines, R. T. (2000) Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A, Eur. J. Biochem, 267, 566-572.
48. Daniel, R. M., Dines, M., and Petach, H. H. (1996) The denaturation and degradation of stable enzymes at high temperatures, Biochem. J. 317, 1-11.
49. Peretz, D., Williamson, R. A., Kaneko, K., Vergara, J., Leclerc, E., Schmitt-Ulms, G., Mehlhorn, I. R., Legname, G., Wormald, M. R., Rudd, P. M., Dwek, R. A., Burton, D. R., and Prusiner, S. B. (2001) Antibodies inhibit prion propagation and clear cell cultures of prion infectivity, Nature 412, 739-743.
50. Ben-Zvi, A. P., and Goloubinoff, P. (2001) Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones, J. Struct. Biol. 135, 84-93.
51. Pappolla, M., Bozner, P., Soto, C., Shao, H., Robakis, N. K., Zagorski, M., Frangione, B., and Ghiso, J. (1998) Inhibition of Alzheimer β-fibrillogenesis by melatonin, J. Biol. Chem. 273, 7185-7188.
52. Soto, C. (2000) Reversion of prion protein conformational changes by synthetic β-sheet breaker peptides, Lancet 355, 192-197.
53. 1H NMR spectroscopy, Proc. Natl. Acad. Sci. U.S.A. 90, 1776-1780.
54. Kendrick, B. S., Carpenter, J. F., Cleland, J. L., and Randolph, T. W. (1998) A transient expansion of the native state precedes aggregation of recombinant human interferon-gamma, Proc. Natl. Acad. Sci. U.S.A. 95, 14142-14146.
55. Denisov, V. P., Jonsson, B.-H., and Halle, B. (1999) Hydration of denatured and molten globule proteins, Nat. Struct. Biol. 6, 253-260.
56. Chiti, F., Mangione, P., Andreola, A., Giorgetti, S., Stefani, M., Dobson, C. M., Bellotti, V., and Taddei, N. (2001) Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin, J. Mol. Biol. 307, 379-391.