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The structure of cross-ß tapes and tubes formed by an octapeptide, aSß1
journal contribution
posted on 2023-06-08, 13:33 authored by Kyle L Morris, Shahin Zibaee, Lin Chen, Michel Goedert, Pawel Sikorski, Louise SerpellLouise SerpellElaborate morphology: The aSß1 peptide, a fragment of a-synuclein, assembles into flat tapes consisting of a peptide bilayer, which can be modeled based on the cross-ß structure found in amyloid proteins. The tapes are stabilized by hydrogen bonding, whilst the amphiphilic nature of the peptide results in the thin bilayer structure. To further stabilize the structure, these tapes may twist to form helical tapes, which subsequently close into nanotubes.
History
Publication status
- Published
File Version
- Accepted version
Journal
Angewandte Chemie International EditionISSN
1433-7851Publisher
Wiley-VCH Verlag BerlinExternal DOI
Issue
8Volume
52Page range
2279-2283Department affiliated with
- Biochemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2013-02-14First Compliant Deposit (FCD) Date
2013-01-22Usage metrics
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