Accessibility navigation


Fibrillisation of ring-closed amyloid peptides

Downloads

Downloads per month over past year

Hamley, I., 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

[img] Text - Accepted Version
· Please see our End User Agreement before downloading.

9Mb

To link to this article 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
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
ID Code:27597
Publisher:The Royal Society of Chemistry

Download Statistics for this item.

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation