Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 619

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

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
Open this paper in CoChat — free account

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.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/nnano.2010.59

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

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

See all 619

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)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.