Abstract
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. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Morris, K. L., Zibaee, S., Chen, L., Goedert, M., Sikorski, P., & Serpell, L. C. (2013). The structure of cross-β tapes and tubes formed by an octapeptide, αsβ1. Angewandte Chemie - International Edition, 52(8), 2279–2283. https://doi.org/10.1002/anie.201207699
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