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


Autoria(s): Castelletto, Valeria; Cheng, Ge; Furzeland, Steve; Atkins, Derek; Hamley, Ian
Data(s)

01/04/2012

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