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Tuning the amino acid sequence of minimalist peptides to present biological signals via charge neutralised self assembly
journal contribution
posted on 2013-01-01, 00:00 authored by A Rodriguez, C Parish, D Nisbet, Richard WilliamsRichard WilliamsNanofibrous 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.
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Journal
Soft matterVolume
9Issue
15Pagination
3915 - 3919Publisher
Royal Society of ChemistryLocation
Cambridge, EnglandPublisher DOI
ISSN
1744-683XeISSN
1744-6848Language
engPublication classification
C1 Refereed article in a scholarly journalUsage metrics
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