Fibrillisation of ring-closed amyloid peptides
Data(s) |
18/04/2012
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Resumo |
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. |
Formato |
text |
Identificador |
http://centaur.reading.ac.uk/27597/1/CrosslinkedNanotubesChemCommRevised.doc Hamley, I. <http://centaur.reading.ac.uk/view/creators/90000472.html>, Cheng, G. <http://centaur.reading.ac.uk/view/creators/90000602.html>, Castelletto, V. <http://centaur.reading.ac.uk/view/creators/90000493.html>, 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 <http://dx.doi.org/10.1039/c2cc17583e> |
Idioma(s) |
en |
Publicador |
The Royal Society of Chemistry |
Relação |
http://centaur.reading.ac.uk/27597/ creatorInternal Hamley, Ian creatorInternal Cheng, Ge creatorInternal Castelletto, Valeria 10.1039/c2cc17583e |
Tipo |
Article PeerReviewed |