Fibrillisation of ring-closed amyloid peptides

Hamley, I. ORCID: https://orcid.org/0000-0002-4549-0926, Cheng, G., Castelletto, V., Handschin, S. and Mezzenga, r. (2012) Fibrillisation of ring-closed amyloid peptides. Chemical Communications, 48 (31). pp. 3757-3759. ISSN 1359-7345 doi: 10.1039/c2cc17583e

Abstract/Summary

Ring-closing olefin metathesis reactions are used to create intramolecularly ring closed peptides or inter-molecularly ring-closed peptide dimers based on a designed amyloid peptide sequence. The uncrosslinked peptide self-assembles into high aspect ratio nanotubes, however ring-closing leads to the formation of fibrillar and twisted/helical ribbon structures.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/27597
Identification Number/DOI	10.1039/c2cc17583e
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Publisher	The Royal Society of Chemistry
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