Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 14, Pages 5468-5473Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1219476110
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Funding
- National Institutes of Health [EB-003151, EB-002026]
- Swiss National Science Foundation [3100A0-108299]
- Maurice E. Muller Institute of Switzerland
- Biotechnology and Biological Sciences Research Council
- Royal Society
- Wellcome Trust
- BBSRC [BB/C00759X/2] Funding Source: UKRI
- EPSRC [EP/J007404/1] Funding Source: UKRI
- MRC [G0200653] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/C00759X/2] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/J007404/1] Funding Source: researchfish
- Medical Research Council [G0200653] Funding Source: researchfish
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The cross-beta amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of beta-sheet filaments. These complex aggregates have remarkable chemical and physical properties, and the conversion of normally soluble functional forms of proteins into amyloid structures is linked to many debilitating human diseases, including several common forms of age-related dementia. Despite their importance, however, cross-beta amyloid fibrils have proved to be recalcitrant to detailed structural analysis. By combining structural constraints from a series of experimental techniques spanning five orders of magnitude in length scale-including magic angle spinning nuclear magnetic resonance spectroscopy, X-ray fiber diffraction, cryoelectron microscopy, scanning transmission electron microscopy, and atomic force microscopy-we report the atomic-resolution (0.5 angstrom) structures of three amyloid polymorphs formed by an 11-residue peptide. These structures reveal the details of the packing interactions by which the constituent beta-strands are assembled hierarchically into protofilaments, filaments, and mature fibrils.
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