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Control of strand registry by attachment of PEG chains to amyloid peptides influences nanostructure

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Castelletto, V., Cheng, G., Furzeland, S., Atkins, D. and Hamley, I. (2012) Control of strand registry by attachment of PEG chains to amyloid peptides influences nanostructure. Soft Matter, 8. pp. 5434-5438. ISSN 1744-683X

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To link to this article DOI: 10.1039/c2sm25546d

Abstract/Summary

The self-assembly in aqueous solution of PEG-peptide conjugates comprising a model amyloid peptide sequence FFKLVFF that contains the Ab(16–20) KLVFF motif is investigated. X-ray diffraction reveals different packing motifs dependent on PEG chain length. This is correlated to remarkable differences in self-assembled nanostructures. The control of strand registry points to a subtle interplay between aromatic stacking, electrostatic and amphiphilic interactions.

Item Type:Article
Refereed:Yes
Divisions:Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:27910
Publisher:Royal Society of Chemistry
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