Time-resolved small-angle x-ray scattering study of the early stage of amyloid formation of an apomyoglobin mutant

Physical Review E - Statistical, Nonlinear, and Soft Matter Physics

Volumn 84, Issue 6, 2011, Pages

  Ortore, Maria Grazia ^a   Spinozzi, Francesco ^a   Vilasi, Silvia ^b   Sirangelo, Ivana ^c   Irace, Gaetano ^c   Shukla, Anuj ^d   Narayanan, Theyencheri ^d   Sinibaldi, Raffaele ^e   Mariani, Paolo ^a  

^a UNIVERSITÀ POLITECNICA DELLE MARCHE   (Italy)

^b UNIVERSITY OF SALERNO   (Italy)

^c SECOND UNIVERSITY OF NAPLES   (Italy)

^d EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^e UNIVERSITY OF CHIETI   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PH; AGGREGATION PROPERTY; AMYLOID FIBRIL; AMYLOID FORMATION; APOMYOGLOBIN; DIVERSE SPECIES; ELONGATED PARTICLES; FIBRIL FORMATION; FIBRILLOGENESIS; FUNCTION OF TIME; GLOBAL FITTING; LAG PHASE; MONOMERIC SPECIES; PH-JUMP; REARRANGEMENT PROCESS; RELATIVE CONCENTRATION; SMALL ANGLE X-RAY SCATTERING; STOPPED FLOW; STRUCTURAL FEATURE; THERAPEUTIC TREATMENTS; TIME-RESOLVED; TRANSIENT SPECIES;

GLYCOPROTEINS; X RAY SCATTERING;

SCATTERING;

EID: 84555178475     PISSN: 15393755     EISSN: 15502376     Source Type: Journal    
DOI: 10.1103/PhysRevE.84.061904     Document Type: Article

References (57)

1. R. W. Carrell and D. A. Lomas, Lancet LANCAO 0140-6736 10.1016/S0140-6736(97)02073-4 350, 134 (1997). (Pubitemid 27313650)
2. J. D. Sipe and A. S. Cohen, J. Struct. Biol. JSBIEM 1047-8477 10.1006/jsbi.2000.4221 130, 88 (2000).
3. C. M. Dobson, Nature (London) NATUAS 0028-0836 10.1038/nature02261 426, 884 (2003). (Pubitemid 38056880)
4. V. N. Uversky and A. L. Fink, eds., Protein Misfolding, Aggregation and Conformational Diseases, Protein Reviews, Vol. 4 (Springer Science + Business Media, New York, 2006), p. 419.
5. R. Nelson, M. R. Sawaya, M. Balbirnie, A. O. Madsen, C. Riekel, R. Grothe, and D. Eisenberg, Nature (London) NATUAS 0028-0836 10.1038/nature03680 435, 773 (2005). (Pubitemid 40839722)
6. R. Nelson and D. Eisenberg, Curr. Opin. Struct. Biol. COSBEF 0959-440X 10.1016/j.sbi.2006.03.007 16, 260 (2006).
7. F. Chiti, P. Webster, N. Taddei, A. Clark, M. Stefani, G. Ramponi, and C. M. Dobson, Proc. Natl. Acad. Sci. USA PNASA6 0027-8424 10.1073/pnas.96.7.3590 96, 3590 (1999). (Pubitemid 29168954)
8. F. Chiti and C. M. Dobson, Annu. Rev. Biochem. ARBOAW 0066-4154 10.1146/annurev.biochem.75.101304.123901 75, 333 (2006). (Pubitemid 44118036)
9. L. Goldschmidt, P. K. Teng, R. Riek, and D. Eisenberg, Proc. Natl. Acad. Sci. USA PNASA6 0027-8424 10.1073/pnas.0915166107 107, 3487 (2010).
10. J. Schnabel, Nature (London) NATUAS 0028-0836 10.1038/464828a 464, 828 (2010).
11. V. N. Uversky, Curr. Alzheimer Res. NATUAS 1567-2050 10.2174/ 156720508784533312 5, 260 (2008). (Pubitemid 351850211)
12. R. Roychaudhuri, M. Yang, M. M. Hoshi, and D. B. Teplow, J. Biol. Chem. JBCHA3 0021-9258 10.1074/jbc.R800036200 284, 4749 (2009).
13. L. Giehm, D. I. Svergun, D. E. Otzen, and B. Vestergaard, Proc. Natl. Acad. Sci. USA PNASA6 0027-8424 10.1073/pnas.1013225108 108, 3246 (2011).
14. R. Wetzel, Acc. Chem. Res. ACHRE4 0001-4842 10.1021/ar050069h 39, 671 (2006).
15. N. Cerda-Costa, A. Esteras-Chopo, F. X. Aviles, L. Serrano, and V. Villegas, J. Mol. Biol. JMOBAK 0022-2836 10.1016/j.jmb.2006.12.007 366, 1351 (2007). (Pubitemid 46186391)
16. P. Marek, S. Mukherjee, M. T. Zanni, and D. P. Raleigh, J. Mol. Biol. JMOBAK 0022-2836 10.1016/j.jmb.2010.05.041 400, 878 (2010).
17. T. Witte, L. A. Haller, E. Luttmann, J. Kruger, G. Fels, and K. Huber, J. Struct. Biol. JSBIEM 1047-8477 10.1016/j.jsb.2007.02.006 159, 71 (2007). (Pubitemid 46880555)
18. T. Ban, K. Yamaguchi, and Y. Goto, Acc. Chem. Res. ACHRE4 0001-4842 10.1021/ar050074l 39, 663 (2006).
19. A. Nayak, M. Sorci, S. Krueger, and G. Belfort, Proteins 18PLAF 0887-3585 10.1002/prot.22169 74, 556 (2009).
20. C. L. P. Oliveira, M. A. Behrens, J. S. Pedersen, K. Erlacher, D. Otzen, and J. S. Pedersen, J. Mol. Biol. JMOBAK 0022-2836 10.1016/j.jmb.2009.01.020 387, 147 (2009).
21. B. Vestergaard, M. Groenning, M. Roessle, J. S. Kastrup, M. de Weert, J. M. Flink, S. Frokjaer, and M. G. D. I. Svergun, PLoS Biol. JMOBAK 1544-9173 10.1371/journal.pbio.0050134 5, e134 (2007). (Pubitemid 46790398)
22. I. Sirangelo, C. Malmo, M. Casillo, A. Mezzogiorno, M. Papa, and G. Irace, J. Biol. Chem. JBCHA3 0021-9258 10.1074/jbc.M207659200 277, 45887 (2002). (Pubitemid 35417569)
23. I. Sirangelo, C. Malmo, C. Iannuzzi, A. Mezzogiorno, M. R. Bianco, M. Papa, and G. Irace, J. Biol. Chem. JBCHA3 0021-9258 10.1074/jbc.M308207200 279, 13183 (2004). (Pubitemid 38445897)
24. C. Iannuzzi, S. Vilasi, M. Portaccio, G. Irace, and I. Sirangelo, Protein Sci. PRCIEI 0961-8368 10.1110/ps.062471107 16, 507 (2007). (Pubitemid 46327561)
25. C. Malmo, S. Vilasi, C. Iannuzzi, S. Tacchi, C. Cametti, G. Irace, and I. Sirangelo, FASEB J. 0892-6638 10.1096/fj.04-3137fje 20, 346 (2006).
26. I. Sirangelo, C. Iannuzzi, S. Vilasi, G. Irace, G. Giuberti, G. Misso, A. D'Alessandro, A. Abbruzzese, and M. Caraglia, J. Cell. Physiol. JCLLAX 0021-9541 10.1002/jcp.21871 221, 412 (2009).
27. I. Sirangelo, S. Tavassi, P. Martelli, R. Casadio, and G. Irace, Euro. J. Biochem. EJBCAI 0014-2956 10.1046/j.1432-1327.2000.01401.x 267, 3937 (2000). (Pubitemid 30436084)
28. D. B. Wetlaufer, Adv. Protein Chem. EJBCAI 0065-3233 10.1016/S0065- 3233(08)60056-X 17, 303 (1962).
29. P. Panine, S. Finet, T. Weiss, and T. Narayanan, Adv. Colloid Interface Sci. ACISB9 0001-8686 10.1016/j.cis.2006.06.003 127, 9 (2006). (Pubitemid 44854783)
30. See Supplemental Material at http://link.aps.org/supplemental/10.1103/ PhysRevE.84.061904 for additional information on the data analysis.
31. F. Spinozzi, http://www.isf.univpm.it/biophysics/software.htm (unpublished).
32. S. Kirkpatrick, C. D. G. Jr., and M. P. Vecchi, Science SCIEAS 0036-8075 10.1126/science.220.4598.671 220, 671 (1983).
33. W. H. Press, S. A. Teukolsky, W. T. Vetterling, and B. P. Flannery, Numerical Recipes: The Art of Scientific Computing (Cambridge University Press, Cambridge, 2007).
34. T. J. Aird, The IMSL Library, Sources and Development of Mathematical Software (Prentice-Hall, Englewood Cliffs, NJ, 1984).
35. I. Pilz, O. Glatter, and O. Kratky, Methods Enzymol. SCIEAS 0076-6879 10.1016/0076-6879(79)61013-3 61, 148 (1979).
36. M. G. Ortore, F. Spinozzi, P. Mariani, A. Paciaroni, L. Barbosa, H. Amenitsch, M. Steinhart, J. Ollivier, and D. Russo, J. R. Soc. Interface SCIEAS 1742-5689 10.1098/rsif.2009.0163.focus 6, S619 (2009).
37. J. Teixeira, J. Appl. Crystallogr. JACGAR 0021-8898 10.1107/ S0021889888000263 21, 781 (1988).
38. Y. Wang, J. Trewhella, and D. P. Goldenberg, J. Mol. Biol. JMOBAK 0022-2836 10.1016/j.jmb.2008.02.009 377, 1576 (2008).
39. J. S. Pedersen and P. Schurtenberger, Macromolecules MAMOBX 0024-9297 10.1021/ma9607630 29, 7602 (1996).
40. S. Cinelli, F. Spinozzi, R. Itri, S. Finet, F. Carsughi, G. Onori, and P. Mariani, Biophys. J. BIOJAU 0006-3495 10.1016/S0006-3495(01)75983-8 81, 35223533 (2001).
41. F. Spinozzi, F. Carsughi, P. Mariani, L. Saturni, S. Bernstorff, S. Cinelli, and G. Onori, J. Phys. Chem. B JPCBFK 1520-6106 10.1021/jp063427m 111, 3822 (2007). (Pubitemid 46724012)
42. R. Khurana, C. Ionescu-Zanetti, M. Pope, J. Li, L. Nielson, M. Ramrez-Alvarado, L. Regan, A. Fink, and S. Carter, Biophys. J. BIOJAU 0006-3495 10.1016/S0006-3495(03)74550-0 85, 1135 (2003).
43. M. G. Ortore, F. Spinozzi, C. Carsughi, P. Mariani, M. Bonetti, and G. Onori, Chem. Phys. Lett.: 10.1016/j.cplett.2005.11.019 418, 342 (2006). (Pubitemid 43121276)
44. M. G. Ortore, R. Sinibaldi, F. Spinozzi, F. Carsughi, D. Clemens, A. Bonincontro, and P. Mariani, J. Phys. Chem. B JPCBFK 1520-6106 10.1021/jp711544u 112, 12881 (2008).
45. R. Sinibaldi, M. G. Ortore, F. Spinozzi, F. Carsughi, H. Frielinghaus, S. Cinelli, G. Onori, and P. Mariani, J. Chem. Phys. JCPSA6 0021-9606 10.1063/1.2735620 126, 235101 (2007). (Pubitemid 47141505)
46. R. Sinibaldi, M. G. Ortore, F. Spinozzi, S. de Souza Funari, J. Teixeira, and P. Mariani, Eur. Biophys. J. EBJOE8 0175-7571 10.1007/s00249-008-0306-z 37, 673 (2008).
47. P. Mariani, F. Spinozzi, F. Federiconi, H. Amenitsch, L. Spindler, and I. Drevensek-Olenik, J. Phys. Chem. B JPCBFK 1520-6106 10.1021/jp809734p 113, 7934 (2009).
48. L. R. S. Barbosa, M. G. Ortore, F. Spinozzi, P. Mariani, S. Bernstorff, and R. Itri, Biophys. J. BIOJAU 0006-3495 10.1016/j.bpj.2009.09.056 98, 147 (2010).
49. A. Guinier and G. Fournet, Small Angle Scattering of X-ray (Wiley, New York, 1955).
50. V. N. Uversky, FEBS J. BIOJAU 1742-464X 10.1111/j.1742-4658.2010.07721.x 277, 2940 (2010).
51. M. Arimon, I. Diez-Perez, M. Kogan, N. Durany, E. Giralt, F. Sanz, and X. Fernandez-Busquets, FASEB J. 0892-6638 10.1096/fj.04-3485cmt 19, 1344 (2005). (Pubitemid 41113717)
52. T. P. J. Knowles, C. A. Waudby, G. L. Devlin, S. I. A. Cohen, A. Aguzzi, M. Vendruscolo, E. M. Terentjev, M. E. Welland, and C. M. Dobson, Science SCIEAS 0036-8075 10.1126/science.1178250 326, 1533 (2009).
53. D. Zhao and J. S. Moore, J. Am. Chem. Soc. JACSAT 0002-7863 10.1021/ja038252y 125, 16294 (2003). (Pubitemid 38020652)
54. C. C. Lee, A. Nayak, A. Sethuraman, G. Belfort, and G. McRae, Biophys. J. BIOJAU 0006-3495 10.1529/biophysj.106.098608 92, 3448 (2007). (Pubitemid 46698637)
55. C. L. Heldt, S. Zhang, and G. Belfort, Proteins 18PLAF 0887-3585 10.1002/prot.22861 79, 92 (2008).
56. A. Orte, N. R. Birkett, R. W. Clarke, G. Devlin, C. M. Dobson, and D. Klenerman, Proc. Natl. Acad. Sci. USA PNASA6 0027-8424 10.1073/pnas.0803086105 105, 14424 (2008).
57. R. Kayed, E. Head, J. L. Thompson, T. M. McIntire, S. C. Milton, C. W. Cotman, and C. G. Glabe, Science SCIEAS 0036-8075 10.1126/science.1079469 300, 486 (2003). (Pubitemid 36444329)