We acknowledge Alzheimer’s Research UK, the BBSRC synthetic components network, the Medical Research Council (UK) (U105184291), and the Multiple System Atrophy Trust (UK) for financial support.
The Structure of Cross-β Tapes and Tubes Formed by an Octapeptide, αSβ1†
Article first published online: 10 JAN 2013
© 2013 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Angewandte Chemie International Edition
Volume 52, Issue 8, pages 2279–2283, February 18, 2013
How to Cite
Morris, K. L., Zibaee, S., Chen, L., Goedert, M., Sikorski, P. and Serpell, L. C. (2013), The Structure of Cross-β Tapes and Tubes Formed by an Octapeptide, αSβ1. Angew. Chem. Int. Ed., 52: 2279–2283. doi: 10.1002/anie.201207699
- Issue published online: 13 FEB 2013
- Article first published online: 10 JAN 2013
- Manuscript Revised: 22 NOV 2012
- Manuscript Received: 24 SEP 2012
- Funded Access
- Medical Research Council (UK). Grant Number: U105184291
- Multiple System Atrophy Trust (UK)
- helical structure;
- X-ray diffraction
Elaborate morphology: The αSβ1 peptide, a fragment of α-synuclein, assembles into flat tapes consisting of a peptide bilayer, which can be modeled based on the cross-β 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.