The Structure of Cross‐β Tapes and Tubes Formed by an Octapeptide, αSβ1

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 resu...

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Detalles Bibliográficos
Autores principales: Morris, Kyle L., Zibaee, Shahin, Chen, Lin, Goedert, Michel, Sikorski, Pawel, Serpell, Louise C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY‐VCH Verlag 2013
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279883/
https://www.ncbi.nlm.nih.gov/pubmed/23307646
http://dx.doi.org/10.1002/anie.201207699
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author Morris, Kyle L.
Zibaee, Shahin
Chen, Lin
Goedert, Michel
Sikorski, Pawel
Serpell, Louise C.
author_facet Morris, Kyle L.
Zibaee, Shahin
Chen, Lin
Goedert, Michel
Sikorski, Pawel
Serpell, Louise C.
author_sort Morris, Kyle L.
collection PubMed
description 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. [Image: see text]
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spelling pubmed-42798832014-12-31 The Structure of Cross‐β Tapes and Tubes Formed by an Octapeptide, αSβ1 Morris, Kyle L. Zibaee, Shahin Chen, Lin Goedert, Michel Sikorski, Pawel Serpell, Louise C. Angew Chem Int Ed Engl Communications 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. [Image: see text] WILEY‐VCH Verlag 2013-02-13 2013-01-10 /pmc/articles/PMC4279883/ /pubmed/23307646 http://dx.doi.org/10.1002/anie.201207699 Text en © 2013 The Authors. Published by Wiley‐VCH Verlag GmbH & Co. KGaA. https://creativecommons.org/licenses/by/4.0/ 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.
spellingShingle Communications
Morris, Kyle L.
Zibaee, Shahin
Chen, Lin
Goedert, Michel
Sikorski, Pawel
Serpell, Louise C.
The Structure of Cross‐β Tapes and Tubes Formed by an Octapeptide, αSβ1
title The Structure of Cross‐β Tapes and Tubes Formed by an Octapeptide, αSβ1
title_full The Structure of Cross‐β Tapes and Tubes Formed by an Octapeptide, αSβ1
title_fullStr The Structure of Cross‐β Tapes and Tubes Formed by an Octapeptide, αSβ1
title_full_unstemmed The Structure of Cross‐β Tapes and Tubes Formed by an Octapeptide, αSβ1
title_short The Structure of Cross‐β Tapes and Tubes Formed by an Octapeptide, αSβ1
title_sort structure of cross‐β tapes and tubes formed by an octapeptide, αsβ1
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279883/
https://www.ncbi.nlm.nih.gov/pubmed/23307646
http://dx.doi.org/10.1002/anie.201207699
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