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. (2012) Control of strand registry by attachment of PEG chains to amyloid peptides influences nanostructure. Soft Matter, 8. pp. 5434-5438. ISSN 1744-683X
To link to this article DOI: 10.1039/c2sm25546d
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.
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