Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils

Soft Matter

Volumn 5, Issue 24, 2009, Pages 5020-5028

  Dunstan, Dave E ^a   Hamilton Brown, Paul ^a   Asimakis, Peter ^a   Ducker, William ^a   Bertolini, Joseph ^b  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b CSL Bioplasma   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER; AMYLOID FIBRIL; AMYLOID PLAQUES; COUETTE; DEMENTIA PATIENTS; FIBRIL STRUCTURE; FORMATION MECHANISM; IN-VITRO; IN-VIVO; LACTOGLOBULIN; LINEAR AGGREGATES; MECHANICAL STRENGTH; MISFOLDED PROTEINS; NANOMECHANICAL PROPERTY; SELF-ASSEMBLE; SHEAR-INDUCED STRUCTURES; TWISTED RIBBON;

ATOMIC FORCE MICROSCOPY; ELASTICITY; MECHANICAL PROPERTIES; MORPHOLOGY; PROTEINS;

GLYCOPROTEINS;

EID: 71749112862     PISSN: 1744683X     EISSN: 17446848     Source Type: Journal    
DOI: 10.1039/b914089a     Document Type: Article

References (54)

1. J. D. Sipe A. S. Cohen Review: history of the amyloid fibril J. Struct. Biol. 2000 130 88 98
2. D. J. Selkoe Folding proteins in fatal ways Nature 2003 426 900 904
3. C. M. Dobson Protein misfolding, evolution and disease Trends Biochem. Sci. 1999 24 329 332
4. 2-microglobulin Nat. Struct. Mol. Biol. 2002 9 326 331
5. F. Chiti N. Taddei M. Bucciantini P. White G. Ramponi C. M. Dobson Mutational analysis of the propensity for amyloid formation by a globular protein EMBO J. 2000 19 1441 1449
6. F. Chiti P. Webster N. Taddei A. Clark M. Stefani G. Ramponi C. M. Dobson Designing conditions for in vitro formation of amyloid protofilaments and fibrils Proc. Natl. Acad. Sci. U. S. A. 1999 96 3590 3594
7. C. M. Dobson Protein folding and misfolding Nature 2003 426 884 890
8. L. C. Serpell Alzheimer's amyloid fibrils: structure and assembly Biochim. Biophys. Acta, Mol. Basis Dis. 2000 1502 16 30
9. M. Sunde C. C. F. Blake From the globular to the fibrous state: protein structure and structural conversion in amyloid formation Q. Rev. Biophys. 1998 31 1 39
10. M. Calamai F. Chiti C. M. Dobson Amyloid fibril formation can proceed from different conformations of a partially unfolded protein Biophys. J. 2005 89 4201 4210
11. S. E. Charm and G. S. Kurland, in Cardiovascular Fluid Dynamics, ed., D. H. Bergel,, Academic Press, London, 1972
12. T. R. Serio A. G. Cashikar A. S. Kowal G. J. Sawicki J. J. Moslehi L. Serpell M. F. Arnsdorf S. L. Lindquist Nucleated conformational conversion and the replication of conformational information by a prion determinant Science 2000 289 1317 1321
13. S. R. Collins A. Douglass R. D. Vale J. S. Weissman Mechanism of prion propagation: amyloid growth occurs by monomer addition PLos Biol. 2004 2 1582 1590
14. A. T. Petkova R. D. Leapman Z. Guo W.-M. Yau M. P. Mattson R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer's beta-Amyloid fibrils Science 2005 307 262 265
15. E. K. Hill B. Krebs D. G. Goodall G. J. Howlett D. E. Dunstan Shear flow induces amyloid fibril formation Biomacromolecules 2006 7 10 13
16. L. Sawyer G. Kontopidis The core lipocalin, bovine β-lactoglobulin Biochim. Biophys. Acta 2000 1482 136 148
17. L. N. Arnaudov R. deVries H. Ippel C. P. M. van Mierlo Multiple steps during the formation of β-lactoglobulin fibrils Biomacromolecules 2003 4 1614 1622
18. P. Aymard T. Nicolai D. Durand A. Clark Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2 Macromolecules 1999 32 2542 2552
19. S. Ikeda V. J. Morris Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy Biomacromolecules 2003 3 382 389
20. W. S. Gosal A. H. Clark S. B. Ross-Murphy Fibrillar β-lactoglobulin gels: Part 1. Fibril formation and structure Biomacromolecules 2004 5 2408 2419
21. E. H. C. Bromley M. R. H. Krebs A. M. Donald Aggregation across the length-scales in β-lactoglobulin Faraday Discuss. 2005 128 13 27
22. D. Hamada C. M. Dobson A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea Protein Sci. 2002 11 2417 2426
23. M. Sunde L. C. Serpell M. Bartlam P. E. Frazer M. B. Pepys C. C. Blake Common core structure of amyloid fibrils by synchrotron X-ray diffraction J. Mol. Biol. 1997 273 729 739 (Pubitemid 27488813)
24. C. McAllister et al Protein interactions and misfolding analyzed by AFM force spectroscopy J. Mol. Biol. 2005 354 1028 1042
25. E. K. Hill R. L. Watson D. E. Dunstan Rheofluorescence technique for the study of dilute MEH-PPV solutions in Couette flow J. Fluoresc. 2005 15 255 266
26. J. E. Sader J. W. Chon P. Mulvaney Calibration of rectangular atomic force microscope cantilevers Rev. Sci. Instrum. 1999 70 3967 3973
27. C. Bustamante J. F. Marko E. D. Siggia S. Smith Entropic elasticity of lambda-phage DNA Science 1994 265 1599 1600
28. L. Whitmore B. A. Wallace DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 2004 32 W668 W673
29. N. Sreerama R. W. Woody Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set Anal. Biochem. 2000 287 252 260
30. N. Sreerama S. Y. Venyaminov R. W. Woody Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis Anal. Biochem. 2000 287 243 251 (Pubitemid 32006233)
31. D. Hamada S. Segawa Y. Goto Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein Nat. Struct. Mol. Biol. 1996 3 868 873
32. A. Touhami J. R. Dutcher pH-induced changes in adsorbed β-lactoglobulin molecules measured using atomic force microscopy Soft Matter 2009 5 220 227
33. J. D. Harper S. S. Wong C. M. Lieber P. T. Lansbury Observation of metastable Abeta amyloid protofibrils by atomic force microscopy Chem. Biol. 1997 4 119 125
34. V. J. Morris, A. R. Kirby and A. P. Gunning, Atomic Force Microscopy for Biologists, Imperial College Press, London, 1999
35. M. Stefani Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world Biochim. Biophys. Acta, Mol. Basis Dis. 2004 1739 5 25
36. H. K. L. Blackley N. Patel M. C. Davies C. J. Roberts S. J. B. Tendler M. J. Wilkinson P. M. Williams Morphological development of beta(1-40) amyloid fibrils Exp. Neurol. 1999 158 437 443
37. A. Lorenzo B. A. Yankner Amyloid fibril toxicity in Alzheimer's disease and diabetes Anal. N. Y. Acad. Sci. 2006 777 89 95
38. M. Bucciantini E. Gionnoni F. Chiti F. Baroni L. Fornigli J. Zurdo N. Tadder G. Ramponi C. M. Dobson M. Stefani Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 2002 416 507 511
39. J. Kim E.-K. Myung I.-H. Lee S. R. Paik Control of morphology and subsequent toxicity of Aβ amyloid fibrils through Dequalinium-induced seed modification Bull. Korean Chem. Soc. 2007 28 2283 2287
40. T. Fukuma A. S. Mostaert S. P. Jarvis Explanation for the mechanical strength of amyloid fibrils Tribol. Lett. 2006 22 233 237
41. A. Karsai Z. Martonfalvi A. Nagy L. Grama B. Penke M. S. Z. Kellermayer Mechanical manipulation of Alzheimer's amyloid beta(1-42) fibrils J. Struct. Biol. 2006 155 316 326
42. A. Karsai A. Nagy A. Kengyel Z. Martonfalvi L. Grama B. Penke M. S. Z. Kellermayer Effect of Lysine-28 side-chain acetylation on the nanomechanical behavior of Alzheimer amyloid-β (25-35) fibrils J. Chem. Inf. Model. 2005 45 1641 1646
43. M. S. Z. Kellermayer L. Grama A. Karsai A. Nagy A. Kahn Z. L. Datki B. Penke Reversible mechanical unzipping of amyloid β-fibrils J. Biol. Chem. 2005 280 8464 8470
44. A. S. Mostaert M. J. Higgins T. Fukuma R. Fabio S. P. Jarvis Nanoscale mechanical characterisation of amyloid fibrils discovered in a natural adhesive J. Biol. Phys. 2006 32 393 401
45. A. S. Mostaert S. P. Jarvis Beneficial characteristics of mechanically functional amyloid fibrils evolutionarily preserved in natural adhesives Nanotechnology 2007 18 044010
46. R. Hertadi F. Gruswitz L. Silver A. Koide S. Koide H. Arakawa A. Ikai Unfolding mechanics of multiple OspA substrates investigated with single molecule force spectroscopy J. Mol. Biol. 2003 333 993 1002
47. T. J. Senden J.-M. di Meglio P. Auroy Anomalous adhesion in adsorbed polymer layers Eur. Phys. J. B 1998 3 211 216
48. A. F. Oberhauser P. E. Marszalek H. P. Erickson J. M. Fernandez The molecular elasticity of the extracellular matrix protein tenascin Nature 1998 393 181 185
49. M. Rief M. Gautel F. Oesterhelt J. M. Fernandez H. E. Gaub Reversible unfolding of individual titin immunoglobulin domains by AFM Science 1997 276 1109 1112
50. M. Fandrich C. M. Dobson The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation EMBO J. 2002 21 5682 5690
51. J. Michele R. Patzold R. Donis Alignment and aggregation effects in suspensions of spheres in non-Newtonian media Rheol. Acta 1977 16 317 321
52. X. Châtellier T. J. Senden J.-F. Joanny J.-M. di Meglio Detachment of a single polyelectrolyte chain adsorbed on a charged surface Europhys. Lett. 1998 41 303 308
53. M. Bouchard J. Zurdo E. J. Nettleton C. M. Dobson C. V. Robinson Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy Protein Sci. 2000 9 1960 1967
54. H. K. L. Blackley G. H. W. Sanders M. C. Davies C. J. Roberts S. J. B. Tendler M. J. Wilkinson In situ atomic force microscopy study of β-amyloid fibrillization J. Mol. Biol. 2000 298 833 840