Issue 20, 2012
From the journal:

Soft Matter

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

Valeria Castelletto,a   Ge Cheng,ac   Steve Furzeland,b   Derek Atkinsb  and  Ian W. Hamley*a  

* Corresponding authors

a Dept of Chemistry, University of Reading, Whiteknights, Reading RG6 6AD, UK
E-mail: I.W.Hamley@reading.ac.uk

b Colworth Discover-Unilever R&D, Sharnbrook MK44 1LQ, UK

c Currently at Department of Chemistry, University of Liverpool, Crown Street, Liverpool L69 7ZD, UK

Abstract

The self-assembly in aqueous solution of PEG-peptide conjugates comprising a model amyloid peptide sequence FFKLVFF that contains the Aβ(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.

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

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Article information

DOI
https://doi.org/10.1039/C2SM25546D
Article type
Communication
Submitted
08 Mar 2012
Accepted
02 Apr 2012
First published
16 Apr 2012

Soft Matter, 2012,8, 5434-5438

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

V. Castelletto, G. Cheng, S. Furzeland, D. Atkins and I. W. Hamley, Soft Matter, 2012, 8, 5434 DOI: 10.1039/C2SM25546D

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