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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 Serpell
Elaborate 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 Edition

ISSN

1433-7851

Publisher

Wiley-VCH Verlag Berlin

Issue

8

Volume

52

Page range

2279-2283

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2013-02-14

First Compliant Deposit (FCD) Date

2013-01-22

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