Atomic structure and hierarchical assembly of a cross-β amyloid fibril
The cross-β amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of β-sheet filaments. These complex aggregates have remarkable chemical and physical properties, and the conversion of normally soluble functional forms of proteins...
| Main Authors: | , , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | en_US |
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National Academy of Sciences (U.S.)
2013
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| Online Access: | http://hdl.handle.net/1721.1/81291 https://orcid.org/0000-0003-1589-832X |
| _version_ | 1826199136447234048 |
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| author | Griffin, Robert Guy Debelouchina, Galia Tzvetanova Bayro, Marvin J. Caporini, Marc A. Bajaj, Vikram S. Jaroniec, Christopher P. Ladizhansky, Vladimir Fitzpatrick, Andrew W. P. Clare, Daniel K. Wang, Luchun Muller, Shirley A. MacPhee, Cait E. Waudby, Christopher A. Mott, Helen R. De Simone, Alfonso Knowles, Tuomas P. J. Saibil, Helen R. Vendruscolo, Michele Orlova, Elena V. Dobson, Christopher M. |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Griffin, Robert Guy Debelouchina, Galia Tzvetanova Bayro, Marvin J. Caporini, Marc A. Bajaj, Vikram S. Jaroniec, Christopher P. Ladizhansky, Vladimir Fitzpatrick, Andrew W. P. Clare, Daniel K. Wang, Luchun Muller, Shirley A. MacPhee, Cait E. Waudby, Christopher A. Mott, Helen R. De Simone, Alfonso Knowles, Tuomas P. J. Saibil, Helen R. Vendruscolo, Michele Orlova, Elena V. Dobson, Christopher M. |
| author_sort | Griffin, Robert Guy |
| collection | MIT |
| description | The cross-β amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of β-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-β 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 Å) structures of three amyloid polymorphs formed by an 11-residue peptide. These structures reveal the details of the packing interactions by which the constituent β-strands are assembled hierarchically into protofilaments, filaments, and mature fibrils. |
| first_indexed | 2024-09-23T11:14:58Z |
| format | Article |
| id | mit-1721.1/81291 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T11:14:58Z |
| publishDate | 2013 |
| publisher | National Academy of Sciences (U.S.) |
| record_format | dspace |
| spelling | mit-1721.1/812912022-10-01T02:21:55Z Atomic structure and hierarchical assembly of a cross-β amyloid fibril Griffin, Robert Guy Debelouchina, Galia Tzvetanova Bayro, Marvin J. Caporini, Marc A. Bajaj, Vikram S. Jaroniec, Christopher P. Ladizhansky, Vladimir Fitzpatrick, Andrew W. P. Clare, Daniel K. Wang, Luchun Muller, Shirley A. MacPhee, Cait E. Waudby, Christopher A. Mott, Helen R. De Simone, Alfonso Knowles, Tuomas P. J. Saibil, Helen R. Vendruscolo, Michele Orlova, Elena V. Dobson, Christopher M. Massachusetts Institute of Technology. Department of Chemistry Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology) Griffin, Robert Guy Debelouchina, Galia Tzvetanova Bayro, Marvin J. Caporini, Marc A. Bajaj, Vikram S. Jaroniec, Christopher P. Ladizhansky, Vladimir The cross-β amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of β-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-β 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 Å) structures of three amyloid polymorphs formed by an 11-residue peptide. These structures reveal the details of the packing interactions by which the constituent β-strands are assembled hierarchically into protofilaments, filaments, and mature fibrils. National Institutes of Health (U.S.) (Grant EB-003151) National Institutes of Health (U.S.) (Grant EB-002026) 2013-10-03T16:43:22Z 2013-10-03T16:43:22Z 2013-03 2012-11 Article http://purl.org/eprint/type/JournalArticle 0027-8424 1091-6490 http://hdl.handle.net/1721.1/81291 Fitzpatrick, A. W. P., G. T. Debelouchina, M. J. Bayro, D. K. Clare, M. A. Caporini, V. S. Bajaj, C. P. Jaroniec, et al. “Atomic structure and hierarchical assembly of a cross- amyloid fibril.” Proceedings of the National Academy of Sciences 110, no. 14 (April 2, 2013): 5468-5473. https://orcid.org/0000-0003-1589-832X en_US http://dx.doi.org/10.1073/pnas.1219476110 Proceedings of the National Academy of Sciences Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf National Academy of Sciences (U.S.) PNAS |
| spellingShingle | Griffin, Robert Guy Debelouchina, Galia Tzvetanova Bayro, Marvin J. Caporini, Marc A. Bajaj, Vikram S. Jaroniec, Christopher P. Ladizhansky, Vladimir Fitzpatrick, Andrew W. P. Clare, Daniel K. Wang, Luchun Muller, Shirley A. MacPhee, Cait E. Waudby, Christopher A. Mott, Helen R. De Simone, Alfonso Knowles, Tuomas P. J. Saibil, Helen R. Vendruscolo, Michele Orlova, Elena V. Dobson, Christopher M. Atomic structure and hierarchical assembly of a cross-β amyloid fibril |
| title | Atomic structure and hierarchical assembly of a cross-β amyloid fibril |
| title_full | Atomic structure and hierarchical assembly of a cross-β amyloid fibril |
| title_fullStr | Atomic structure and hierarchical assembly of a cross-β amyloid fibril |
| title_full_unstemmed | Atomic structure and hierarchical assembly of a cross-β amyloid fibril |
| title_short | Atomic structure and hierarchical assembly of a cross-β amyloid fibril |
| title_sort | atomic structure and hierarchical assembly of a cross β amyloid fibril |
| url | http://hdl.handle.net/1721.1/81291 https://orcid.org/0000-0003-1589-832X |
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