Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
- Adamcik, Jozef Laboratoire de Physique de la Matière Vivante, Ecole Polytechnique Fédérale de Lausanne (EPFL), Switzerland
- Jung, Jin-Mi Department of Physics and Fribourg Center for Nanomaterials, University of Fribourg, Switzerland
- Flakowski, Jérôme Laboratoire de Biophysique Statistique, Ecole Polytechnique Fédérale de Lausanne (EPFL), Switzerland
- Rios, Paolo De Los Laboratoire de Biophysique Statistique, Ecole Polytechnique Fédérale de Lausanne (EPFL), Switzerland
- Dietler, Giovanni Laboratoire de Physique de la Matière Vivante, Ecole Polytechnique Fédérale de Lausanne (EPFL), Switzerland
- Mezzenga, Raffaele ETH Zurich, Food & Soft Materials Science, Institute of Food, Nutrition & Health, Switzerland
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11.04.2010
Published in:
- Nature Nanotechnology. - 2010, vol. 5, p. 423 - 428
English
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 β-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.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Physique
- Language
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- English
- Classification
- Physics
- License
- License undefined
- Identifiers
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- RERO DOC 20624
- DOI 10.1038/nnano.2010.59
- Persistent URL
- https://folia.unifr.ch/unifr/documents/301764
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