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Molecular basis for amyloid fibril formation and stability
journal contribution
posted on 2023-06-08, 06:09 authored by O Sumner Makin, Edward Atkins, Pawel Sikorski, Jan Johansson, Louise SerpellLouise SerpellThe molecular structure of the amyloid fibril has remained elusive because of the difficulty of growing well diffracting crystals. By using a sequence-designed polypeptide, we have produced crystals of an amyloid fiber. These crystals diffract to high resolution (1 Å) by electron and x-ray diffraction, enabling us to determine a detailed structure for amyloid. The structure reveals that the polypeptides form fibrous crystals composed of antiparallel ß-sheets in a cross-ß arrangement, characteristic of all amyloid fibers, and allows us to determine the side-chain packing within an amyloid fiber. The antiparallel ß-sheets are zipped together by means of p-bonding between adjacent phenylalanine rings and salt-bridges between charge pairs (glutamic acid¿lysine), thus controlling and stabilizing the structure. These interactions are likely to be important in the formation and stability of other amyloid fibrils.
History
Publication status
- Published
Journal
Proceedings of the National Academy of SciencesISSN
0027-8424Publisher
National Academy of SciencesExternal DOI
Issue
2Volume
102Page range
315-320Pages
6.0Department affiliated with
- Biochemistry Publications
Notes
Senior Author (LS). First author (student OSM). LS directed the research, wrote the paper and is corresponding author. OSM carried out the research and co-authored the paper. This was the first molecular structure of an amyloid fibril, solved by fibre diffraction and modelling, cited 97 times.Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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