Control of strand registry by attachment of PEG chains to amyloid peptides influences nanostructure
Data(s) |
01/04/2012
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Resumo |
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. |
Formato |
text text |
Identificador |
http://centaur.reading.ac.uk/27910/2/CG101SoftMatterRevised.doc http://centaur.reading.ac.uk/27910/3/CG101SoftMatterRevised.pdf Castelletto, V. <http://centaur.reading.ac.uk/view/creators/90000493.html>, Cheng, G. <http://centaur.reading.ac.uk/view/creators/90000602.html>, Furzeland, S., Atkins, D. and Hamley, I. <http://centaur.reading.ac.uk/view/creators/90000472.html> (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 <http://dx.doi.org/10.1039/c2sm25546d> |
Idioma(s) |
en en |
Publicador |
Royal Society of Chemistry |
Relação |
http://centaur.reading.ac.uk/27910/ creatorInternal Castelletto, Valeria creatorInternal Cheng, Ge creatorInternal Hamley, Ian 10.1039/c2sm25546d |
Tipo |
Article PeerReviewed |