Tuning the amino acid sequence of minimalist peptides to present biological signals via charge neutralised self assembly

Rodriguez, Alexandra L., Parish, Clare L., Nisbet, David R. and Williams, Richard J. 2013, Tuning the amino acid sequence of minimalist peptides to present biological signals via charge neutralised self assembly, Soft matter, vol. 9, no. 15, pp. 3915-3919.

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Title Tuning the amino acid sequence of minimalist peptides to present biological signals via charge neutralised self assembly
Author(s) Rodriguez, Alexandra L.
Parish, Clare L.
Nisbet, David R.
Williams, Richard J.
Journal name Soft matter
Volume number 9
Issue number 15
Start page 3915
End page 3919
Total pages 5
Publisher Royal Society of Chemistry
Place of publication Cambridge, England
Publication date 2013
ISSN 1744-683X
1744-6848
Summary Nanofibrous materials yielded by the self-assembly of peptides are rich in potential; particularly for the formation of scaffolds that mimic the landscape of the host environment of the cell. Here, we report a novel methodology to direct the formation of supramolecular structures presenting desirable amino acid sequences by the self-assembly of minimalist peptides which cannot otherwise yield the desired scaffold structures under biologically relevant conditions. Through the rational modification of the pK?, we were able to optimise ordered charge neutralised assembly towards in vivo conditions.
Language eng
Field of Research 059999 Environmental Sciences not elsewhere classified
Socio Economic Objective 970105 Expanding Knowledge in the Environmental Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Persistent URL http://hdl.handle.net/10536/DRO/DU:30057693

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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