Kinetic analysis of amyloid protofibril dissociation and volumetric properties of the transition state

Biophysical Journal

Volumn 92, Issue 1, 2007, Pages 323-329

  Abdul Latif, Abdul Raziq ^a   Kono, Ryohei ^a   Tachibana, Hideki ^b   Akasaka, Kazuyuki ^a  

^a KINKI UNIVERSITY   (Japan)

^b KOBE UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; LYSOZYME; MONOMER;

ARTICLE; ATOMIC FORCE MICROSCOPY; DISSOCIATION; FIBER; KINETICS; POLYMERIZATION;

EID: 33846014251     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.088120     Document Type: Article

References (28)

1. Dobson, C. M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:329-332.
2. Koo, E. H., P. T. Lansbury, and J. W. Kelly. 1999. Amyloid disease; abnormal protein aggregation in neurodegeneration. Proc. Natl. Acad. Sci. USA. 96:9989-9990.
3. Dubois, J., A. A. Ismail, S. L. Chan, and Z. Ali-Khan. 1999. Fourier transform infrared spectroscopic investigation of temperature- and pressure-induced disaggregation of amyloid A. Scand. J. Immunol. 49:376-380.
4. Foguel, D., M. C. Suarez, A. D. Ferrao-Gonzales, T. C. Porto, L. Palmieri, C. M. Einsiedler, L. R. Andrade, H. A. Lashuel, P. T. Lansbury, J. W. Kelly, and J. L. Silva. 2003. Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities. Proc. Natl. Acad. Sci. USA. 100:9831-9836.
5. Seefeldt, M. B., J. Ouyang, W. A. Froland, J. F. Carpenter, and T. W. Randolph. 2004. High-pressure refolding of bikunin; efficacy and thermodynamics. Protein Sci. 13:2639-2650.
6. Carulla, N., G. L. Caddy, D. R. Hall, J. Zurdo, M. Gairi, M. Feliz, and E. Giralt. 2005. Molecular recycling within amyloid fibrils. Nature. 436:554-558.
7. Tachibana, H. 2000. Propensities for the formation of individual disulfide bonds in hen lysozyme and in the size and stability of disulfide-associated submolecular structure. FEBS Lett. 480:175-178.
8. Niraula, T. N., T. Konno, H. Li, H. Yamada, K. Akasaka, and H. Tachibana. 2004. Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils. Proc. Natl. Acad. Sci. USA. 101:4089-4093.
9. Kamatari, Y. O., S. Yokoyama, H. Tachibana, and K. Akasaka. 2005. Pressure-jump NMR study of dissociation and association of amyloid protofibrils. J. Mol. Biol. 349:916-921.
10. Oosawa, F., and S. Asakura. 1975. Thermodynamics of the Polymerization of Protein. Academic Press, London, UK.
11. Imoto, T., L. S. Forster, J. A. Rupley, and F. Tanaka. 1972. Fluorescence of lysozyme; emissions from tryptophan residues 62 and 108 and energy migration. Proc. Natl. Acad. Sci. USA. 69:1151-1155.
12. Goldsbury, C., J. Kistler, U. Aebi, T. Arvinte, and G. J. S. Cooper. 1999. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J. Mol. Biol. 285:33-39.
13. Blackley, H. K. L., G. H. W. Sanders, M. C. Davies, C. J. Roberts, S. J. B. Tendler, and M. J. Wilkinson. 2000. In-situ atomic force microscopy study of β-amyloid fibrillization. J. Mol. Biol. 298:833-840.
14. Scheibel, T., A. S. Kowal, J. D. Bloom, and S. L. Lindquist. 2001. Bidirectional amyloid fiber growth for a yeast prion determinant. Curr. Biol. 11:366-369.
15. Inoue, Y., A. Kishimoto, J. Hirao, M. Yoshida, and H. Taguchi. 2001. Strong growth polarity of yeast prion fiber revealed by single fiber imaging. J. Biol. Chem. 276:35227-35230.
16. Ban, T., D. Hamada, K. Hasegawa, H. Naiki, and Y. Goto. 2003. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J. Biol. Chem. 278:16462-16465.
17. Royer, C. A. 2002. Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta. 1595:201-209.
18. Zipp, A., and W. Kauzmann. 1973. Pressure denaturation of metmyoglobin. Biochemistry. 12:4217-4228.
19. Li, T. M., J. W. Hook, H. G. Drickamer, and G. Weber. 1976. Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme. Biochemistry. 15:5571-5580.
20. 1H-NMR spectroscopy. Proc. Natl. Acad. Sci. USA. 90:1776-1780.
21. Samarasinghe, S. D., D. M. Campbell, and J. J. Jonas. 1992. High-resolution NMR study of the pressure-induced unfolding of lysozyme. Biochemistry. 31:7773-7778.
22. Hawley, S. A. 1971. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry. 10:2436-2442.
23. Prehoda, K. E., E. S. Moorberry, and J. L. Markley. 1998. Pressure denaturation of proteins: evaluation of compressibility effects. Biochemistry. 37:5785-5790.
24. Lassalle, M. W., H. Yamada, and K. Akasaka. 2000. The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by 1H-NMR. J. Mol. Biol. 298:293-302.
25. Seemann, H., R. Winter, and C. A. Royer. 2001. Volume expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of Staphylococcal nuclease. J. Mol. Biol. 307:1091-1102.
26. Chalikian, T. V., and K. J. Breslauer. 1996. On volume changes accompanying conformational transitions of biopolymers. Proc. Natl. Acad. Sci. USA. 93:1012-1014.
27. Taulier, N., and T. V. Chalikian. 2002. Compressibility of protein transitions. Biochim. Biophys. Acta. 1595:48-70.
28. Korzhnev, D. M., I. Bezsonova, F. Evanics, N. Taulier, Z. Zhou, Y. Bai, T. V. Chalikian, R. S. Prosser, and L. E. Kay. 2006. Probing the transition state ensemble of a protein folding reaction by pressure-dependent NMR relaxation dispersion. J. Am. Chem. Soc. 128:5262-5269.