Solubility and supersaturation-dependent protein misfolding revealed by ultrasonication

Langmuir

Volumn 30, Issue 7, 2014, Pages 1845-1854

  Lin, Yuxi ^a   Lee, Young Ho ^a   Yoshimura, Yuichi ^a   Yagi, Hisashi ^a   Goto, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DERIVATIVE; EGG WHITE; LYSOZYME; WATER;

ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CHICKEN; METABOLISM; PROTEIN DENATURATION; PROTEIN FOLDING; SOLUBILITY; ULTRASOUND;

ALCOHOLS; ANIMALS; CHICKENS; EGG WHITE; MODELS, MOLECULAR; MURAMIDASE; PROTEIN DENATURATION; PROTEIN FOLDING; SOLUBILITY; SONICATION; WATER;

EID: 84894669883     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la403100h     Document Type: Article

References (57)

1. Shiraki, K.; Nishikawa, K.; Goto, Y. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding J. Mol. Biol. 1995, 245, 180-194
2. Hirota, N.; Mizuno, K.; Goto, Y. Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol Protein Sci. 1997, 6, 416-421
3. Buck, M. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins Q. Rev. Biophys. 1998, 31, 297-355
4. Hong, D. P.; Hoshino, M.; Kuboi, R.; Goto, Y. Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides J. Am. Chem. Soc. 1999, 121, 8427-8433
5. Hoshino, M.; Hagihara, Y.; Hamada, D.; Kataoka, M.; Goto, Y. Trifluoroethanol-induced conformational transition of hen egg-white lysozyme studied by small-angle X-ray scattering FEBS Lett. 1997, 416, 72-76
6. Yanagi, K.; Ashizaki, M.; Yagi, H.; Sakurai, K.; Lee, Y. H.; Goto, Y. Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions J. Biol. Chem. 2011, 286, 23959-23966
7. Cohn, E. J.; Strong, L. E.; Hughes, W. L.; Mulford, D. J.; Ashworth, J. N.; Melin, M.; Taylor, H. L. Preparation and properties of serum and plasma proteins. 4. A system for the separation into fractions of the protein and lipoprotein components of biological tissues and fluids J. Am. Chem. Soc. 1946, 68, 459-475
8. 2-microglobulin-related amyloid fibrils at a neutral pH J. Am. Soc. Nephrol. 2004, 15, 126-133
9. Chiti, F.; Taddei, N.; Bucciantini, M.; White, P.; Ramponi, G.; Dobson, C. M. Mutational analysis of the propensity for amyloid formation by a globular protein EMBO J. 2000, 19, 1441-1449
10. 2-microglobulin fragment are induced by fluorine-substituted alcohols J. Mol. Biol. 2006, 363, 279-288
11. Anderson, V. L.; Webb, W. W. A desolvation model for trifluoroethanol- induced aggregation of enhanced green fluorescent protein Biophys. J. 2012, 102, 897-906
12. Pallares, I.; Vendrell, J.; Aviles, F. X.; Ventura, S. Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin J. Mol. Biol. 2004, 342, 321-331
13. Srisailam, S.; Kumar, T. K.; Rajalingam, D.; Kathir, K. M.; Sheu, H. S.; Jan, F. J.; Chao, P. C.; Yu, C. Amyloid-like fibril formation in an all β-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation J. Biol. Chem. 2003, 278, 17701-17709
14. 2-microglobulin J. Mol. Biol. 2010, 401, 286-297
15. Fezoui, Y.; Teplow, D. B. Kinetic studies of amyloid β-protein fibril assembly. Differential effects of α-helix stabilization J. Biol. Chem. 2002, 277, 36948-36954
16. Chatani, E.; Yagi, H.; Naiki, H.; Goto, Y. Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanol J. Biol. Chem. 2012, 287, 22827-22837
17. Kumar, S.; Udgaonkar, J. B. Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein Biochemistry 2009, 48, 6441-6449
18. Sekhar, A.; Udgaonkar, J. B. Fluoroalcohol-induced modulation of the pathway of amyloid protofibril formation by barstar Biochemistry 2011, 50, 805-819
19. Plakoutsi, G.; Taddei, N.; Stefani, M.; Chiti, F. Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation J. Biol. Chem. 2004, 279, 14111-14119
20. Barrow, C. J.; Yasuda, A.; Kenny, P. T.; Zagorski, M. G. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease. Analysis of circular dichroism spectra J. Mol. Biol. 1992, 225, 1075-1093
21. Cohen, F. E.; Kelly, J. W. Therapeutic approaches to protein-misfolding diseases Nature 2003, 426, 905-909
22. Chiti, F.; Dobson, C. M. Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 2006, 75, 333-366
23. Uversky, V. N.; Fink, A. L. Conformational constraints for amyloid fibrillation: The importance of being unfolded Biochim. Biophys. Acta 2004, 1698, 131-153
24. Sipe, J. D.; Benson, M. D.; Buxbaum, J. N.; Ikeda, S.; Merlini, G.; Saraiva, M. J.; Westermark, P. Amyloid fibril protein nomenclature: 2012 recommendations from the Nomenclature Committee of the International Society of Amyloidosis Amyloid 2012, 19, 167-170
25. Fowler, D. M.; Koulov, A. V.; Balch, W. E.; Kelly, J. W. Functional amyloid-from bacteria to humans Trends. Biochem. Sci. 2007, 32, 217-224
26. Maji, S. K.; Perrin, M. H.; Sawaya, M. R.; Jessberger, S.; Vadodaria, K.; Rissman, R. A.; Singru, P. S.; Nilsson, K. P.; Simon, R.; Schubert, D.; Eisenberg, D.; Rivier, J.; Sawchenko, P.; Vale, W.; Riek, R. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules Science 2009, 325, 328-332
27. Goda, S.; Takano, K.; Yamagata, Y.; Nagata, R.; Akutsu, H.; Maki, S.; Namba, K.; Yutani, K. Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution Protein Sci. 2000, 9, 369-375
28. Poulsen, S. A.; Watson, A. A.; Fairlie, D. P.; Craik, D. J. Solution structures in aqueous SDS micelles of two amyloid β peptides of Aβ(1-28) mutated at the α-secretase cleavage site (K16E, K16F) J. Struct. Biol. 2000, 130, 142-152
29. 2-microglobulin-related amyloid fibrils at a neutral pH Biochemistry 2004, 43, 11075-11082
30. Giehm, L.; Oliveira, C. L. P.; Christiansen, G.; Pedersen, J. S.; Otzen, D. E. SDS-induced fibrillation of α-synuclein: an alternative fibrillation pathway J. Mol. Biol. 2010, 401, 115-133
31. Rivers, R. C.; Kumita, J. R.; Tartaglia, G. G.; Dedmon, M. M.; Pawar, A.; Vendruscolo, M.; Dobson, C. M.; Christodoulou, J. Molecular determinants of the aggregation behavior of α- and β-synuclein Protein Sci. 2008, 17, 887-898
32. Lind, J.; Lindahl, E.; Peralvarez-Marin, A.; Holmlund, A.; Jornvall, H.; Maler, L. Structural features of proinsulin C-peptide oligomeric and amyloid states FEBS J. 2010, 277, 3759-3768
33. Wahlstrom, A.; Hugonin, L.; Peralvarez-Marin, A.; Jarvet, J.; Graslund, A. Secondary structure conversions of Alzheimer's Aβ(1-40) peptide induced by membrane-mimicking detergents FEBS J. 2008, 275, 5117-5128
34. Stohr, J.; Weinmann, N.; Wille, H.; Kaimann, T.; Nagel-Steger, L.; Birkmann, E.; Panza, G.; Prusiner, S. B.; Eigen, M.; Riesner, D. Mechanisms of prion protein assembly into amyloid Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 2409-2414
35. Kumar, S.; Ravi, V. K.; Swaminathan, R. How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates? Biochem. J. 2008, 415, 275-288
36. Ferreon, A. C.; Gambin, Y.; Lemke, E. A.; Deniz, A. A. Interplay of α-synuclein binding and conformational switching probed by single-molecule fluorescence Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 5645-5650
37. Yoshimura, Y.; Lin, Y. X.; Yagi, H.; Lee, Y. H.; Kitayama, H.; Sakurai, K.; So, M.; Ogi, H.; Naiki, H.; Goto, Y. Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 14446-14451
38. Vekilov, P. G. Phase diagrams and kinetics of phase transitions in protein solutions J. Phys.: Condens. Matter 2012, 24, 193101
39. Erdemir, D.; Lee, A. Y.; Myerson, A. S. Nucleation of crystals from solution: classical and two-step models Acc. Chem. Res. 2009, 42, 621-629
40. Oosawa, F.; Kasai, M. A theory of linear and helical aggregations of macromolecules J. Mol. Biol. 1962, 4, 10-21
41. Sawaya, M. R.; Sambashivan, S.; Nelson, R.; Ivanova, M. I.; Sievers, S. A.; Apostol, M. I.; Thompson, M. J.; Balbirnie, M.; Wiltzius, J. J.; McFarlane, H. T.; Madsen, A. O.; Riekel, C.; Eisenberg, D. Atomic structures of amyloid cross-β spines reveal varied steric zippers Nature 2007, 447, 453-457
42. Reches, M.; Gazit, E. Casting metal nanowires within discrete self-assembled peptide nanotubes Science 2003, 300, 625-627
43. Ramshini, H.; Parrini, C.; Relini, A.; Zampagni, M.; Mannini, B.; Pesce, A.; Saboury, A. A.; Nemat-Gorgani, M.; Chiti, F. Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils PLoS One 2011, 6, e16075
44. Auer, S.; Kashchiev, D. Insight into the correlation between lag time and aggregation rate in the kinetics of protein aggregation Proteins 2010, 78, 2412-2416
45. Harper, J. D.; Lansbury, P. T., Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 1997, 66, 385-407
46. Yoshikawa, H.; Hirano, A.; Arakawa, T.; Shiraki, K. Mechanistic insights into protein precipitation by alcohol Int. J. Biol. Macromol. 2012, 50, 865-871
47. Pace, C. N.; Trevino, S.; Prabhakaran, E.; Scholtz, J. M. Protein structure, stability and solubility in water and other solvents Philos. Trans. R. Soc. London, Ser. B 2004, 359, 1225-1234
48. 2-microglobulin J. Biol. Chem. 2005, 280, 32843-32848
49. Chatani, E.; Lee, Y. H.; Yagi, H.; Yoshimura, Y.; Naiki, H.; Goto, Y. Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 11119-11124
50. So, M.; Yagi, H.; Sakurai, K.; Ogi, H.; Naiki, H.; Goto, Y. Ultrasonication-dependent acceleration of amyloid fibril formation J. Mol. Biol. 2011, 412, 568-577
51. Yoshimura, Y.; So, M.; Yagi, H.; Goto, Y. Ultrasonication: an efficient agitation for accelerating the supersaturation-limited amyloid fibrillation of proteins Jpn. J. Appl. Phys. 2013, 52, 07HA01
52. Aune, K. C.; Tanford, C. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Depdendence on pH at 25 degrees Biochemistry 1969, 8, 4579-4585
53. Yonezawa, Y.; Tanaka, S.; Kubota, T.; Wakabayashi, K.; Yutani, K.; Fujiwara, S. An insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle X-ray and neutron scattering study J. Mol. Biol. 2002, 323, 237-251
54. Holley, M.; Eginton, C.; Schaefer, D.; Brown, L. R. Characterization of amyloidogenesis of hen egg lysozyme in concentrated ethanol solution Biochem. Biophys. Res. Commun. 2008, 373, 164-168
55. Huang, K. Y.; Amodeo, G. A.; Tong, L.; McDermott, A. The structure of human ubiquitin in 2-methyl-2,4-pentanediol: a new conformational switch Protein Sci. 2011, 20, 630-639
56. Bryngelson, J. D.; Onuchic, J. N.; Socci, N. D.; Wolynes, P. G. Funnels, pathways, and the energy landscape of protein folding: a synthesis Proteins 1995, 21, 167-195
57. Nymeyer, H.; Garcia, A. E.; Onuchic, J. N. Folding funnels and frustration in off-lattice minimalist protein landscapes Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 5921-5928