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

Castelletto, V., Cheng, G., Furzeland, S., Atkins, D. and Hamley, I. ORCID: https://orcid.org/0000-0002-4549-0926 (2012) Control of strand registry by attachment of PEG chains to amyloid peptides influences nanostructure. Soft Matter, 8. pp. 5434-5438. ISSN 1744-683X 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
URI	https://reading-clone.eprints-hosting.org/id/eprint/27910
Identification Number/DOI	10.1039/c2sm25546d
Refereed	Yes
Divisions	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	Royal Society of Chemistry
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