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Cited by 619

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Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

Open access
Adamcik, Jozef, Jung, Jin-Mi, Flakowski, Jérôme, De Los Rios, Paolo, Dietler, Giovanni, Mezzenga, Raffaele·2010·Nature Nanotechnology
DOI 10.1038/nnano.2010.59
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Abstract

The aggregation of proteins is central to many aspects of daily life, including food processing, blood coagulation, eye cataract formation disease and prion-related neurodegenerative infections. However, the physical mechanisms responsible for amyloidosis-the irreversible fibril formation of various proteins that is linked to disorders such as Alzheimer's, Creutzfeldt-Jakob and Huntington's diseases-have not yet been fully elucidated. Here, we show that different stages of amyloid aggregation can be examined by performing a statistical polymer physics analysis of single-molecule atomic force microscopy images of heat-denatured beta-lactoglobulin fibrils. The atomic force microscopy analysis, supported by theoretical arguments, reveals that the fibrils have a multistranded helical shape with twisted ribbon-like structures. Our results also indicate a possible general model for amyloid fibril assembly and illustrate the potential of this approach for investigating fibrillar systems.

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Research works printed but not linked: 31

  1. Stradner, A. et al. Equilibrium cluster formation in concentrated protein solutions and colloids. Nature 432, 492–495 (2004). · DOI · Paper page
  2. Mezzenga, R., Schurtenberger, P., Burbidge, A. & Michel, M. Understanding foods as soft materials. Nature Mater. 4, 729–740 (2005). · DOI · Paper page
  3. Selkoe, D. J. Folding proteins in fatal ways. Nature 426, 900–904 (2003). · DOI · Paper page
  4. Chiti, F. & Dobson, C. M. Amyloid formation by globular proteins under native conditions. Nature Chem. Biol. 5, 15–22 (2009). · DOI · Paper page
  5. Knowles, T. P. et al. Role of intermolecular forces in defining material properties of protein nanofibrils. Science 318, 1900–1903 (2007). · DOI · Paper page
  6. Nelson, R. et al. Structure of the cross-beta spine of amyloid-like fibrils. Nature 435, 773–778 (2005). · DOI · Paper page
  7. Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid and human disease. Annu. Rev. Biochem. 75, 333–366 (2006). · DOI · Paper page
  8. Graumann, P. L. Cytoskeletal elements in bacteria. Annu. Rev. Microbiol. 61, 589–618 (2007). · DOI
  9. Kueh, H. Y. & Mitchison, T. J. Structural plasticity in actin and tubulin polymer dynamics. Science 325, 960–963 (2009). · DOI · Paper page
  10. Pearce, F. G., Mackintosh, S. H. & Gerrard, J. A. Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing. J. Agric. Food Chem. 55, 318–322 (2007). · DOI
  11. Kavanagh, G. M., Clark, A. H. & Ross-Murphy, S. B. Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels. Int. J. Biol. Macromol. 28, 41–50 (2000). · DOI
  12. Bolder, S. G., Sagis, L. M., Venema, P. & van der Linden, E. Effect of stirring and seeding on whey protein fibril formation. J. Agric. Food Chem. 55, 5661–5669 (2007). · DOI
  13. Gosal, W. S., Clark, A. H. & Ross-Murphy, S. B. Fibrillar beta-lactoglobulin gels: Part 1. Fibril formation and structure. Biomacromolecules 5, 2408–2419 (2004). · DOI
  14. Jung, J. M., Savin, G., Pouzot, M., Schmitt, C. & Mezzenga, R. Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate. Biomacromolecules 9, 2477–2486 (2008). · DOI · Paper page
  15. Gosal, W. S., Clark, A. H., Pudney, P. D. A. & Ross-Murphy, S. B. Novel amyloid fibrillar networks derived from a globular protein: beta-lactoglobulin. Langmuir 18, 7174–7181 (2002). · DOI
  16. Veerman, C., Ruis, H., Sagis, L. M. & van der Linden, E. Effect of electrostatic interactions on the percolation concentration of fibrillar beta-lactoglobulin gels. Biomacromolecules 3, 869–873 (2002). · DOI
  17. Arnaudov, L. N., de Vries, R., Ippel, H. & van Mierlo, C. P. Multiple steps during the formation of beta-lactoglobulin fibrils. Biomacromolecules 4, 1614–1622 (2003). · DOI
  18. Bromley, E. H., Krebs, M. R. & Donald, A. M. Aggregation across the length-scales in beta-lactoglobulin. Faraday Discuss. 128, 13–27 (2005). · DOI
  19. Sagis, L. M., Veerman, C. & van der Linden, E. Mesoscopic properties of semiflexible amyloid fibrils. Langmuir 20, 924–927 (2004). · DOI
  20. Arnaudov, L. N. & de Vries, R. Strong impact of ionic strength on the kinetics of fibrilar aggregation of bovine beta-lactoglobulin. Biomacromolecules 7, 3490–3498 (2006). · DOI
  21. Nilsson, M. R. Techniques to study amyloid fibril formation in vitro. Methods 34, 151–160 (2004). · DOI · Paper page
  22. Lashuel, H. A. & Wall, J. S. Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis. Methods Mol. Biol. 299, 81–101 (2005).
  23. Ikeda, S. & Morris, V. J. Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy. Biomacromolecules 3, 382–389 (2002). · DOI
  24. Chamberlain, A. K. et al. Ultrastructural organization of amyloid fibrils by atomic force microscopy. Biophys. J. 79, 3282–3293 (2000). · DOI
  25. Khurana, R. et al. A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy. Biophys. J. 85, 1135–1144 (2003). · DOI · Paper page
  26. Witz, G., Rechendorff, K., Adamcik, J. & Dietler, G. Conformation of circular DNA in two dimensions. Phys. Rev. Lett. 101, 148103 (2008). · DOI
  27. Manning, G. S. Correlation of polymer persistence length with Euler buckling. Phys. Rev. A 34, 4467–4468 (1986). · DOI
  28. Aggeli, A. et al. Hierarchical self-assembly of chiral rod-like molecules as a model for peptide beta-sheet tapes, ribbons, fibrils and fibers. Proc. Natl Acad. Sci. USA 98, 11857–11862 (2001). · DOI · Paper page
  29. Paravastu, A. K., Leapman, R. D., Yau, W. M. & Tycko, R. Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils. Proc. Natl Acad. Sci. USA 105, 18349–18354 (2008). · DOI · Paper page
  30. Jung, J. M. & Mezzenga, R. Liquid crystalline phase behavior of protein fibers in water: experiments versus theory. Langmuir 26, 504–514 (2010). · DOI
  31. Marek, J. et al. Interactive measurement and characterization of DNA molecules by analysis of AFM images. Cytometry A 63, 87–93 (2005). · DOI

Cited by

Metadata

Authors
Adamcik, J., Jung, J.-M., Flakowski, J., De Los Rios, P., Dietler, G., & Mezzenga, R.
Venue
Nature Nanotechnology
Publisher
Springer Science and Business Media LLC
Published
2010-04-11
Volume
5
Issue
6
Pages
423-428
ISSN
  • 1748-3387 (ISSN-L)
  • 1748-3395
DOI
10.1038/nnano.2010.59
OpenAlex
W2011011528
Cited by
619
References
2
FWCI
20.35
Type
journal article
Language
en
Open access
green
Licence
www.springer.com/tdm (tdm)

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