Disruption of diphenylalanine assembly by a Boc-modified variant

Creasey, Rhiannon C. G., Louzao, Iria, Arnon, Zohar A., Marco, Pini, Adler-Abramovich, Lihi, Roberts, Clive J., Gazit, Ehud and Tendler, Saul J. B. (2016) Disruption of diphenylalanine assembly by a Boc-modified variant. Soft Matter, 12 47: 9451-9457. doi:10.1039/c6sm01770c


Author Creasey, Rhiannon C. G.
Louzao, Iria
Arnon, Zohar A.
Marco, Pini
Adler-Abramovich, Lihi
Roberts, Clive J.
Gazit, Ehud
Tendler, Saul J. B.
Title Disruption of diphenylalanine assembly by a Boc-modified variant
Journal name Soft Matter   Check publisher's open access policy
ISSN 1744-6848
1744-683X
Publication date 2016-12-21
Year available 2016
Sub-type Article (original research)
DOI 10.1039/c6sm01770c
Open Access Status Not yet assessed
Volume 12
Issue 47
Start page 9451
End page 9457
Total pages 7
Place of publication Cambridge, United Kingdom
Publisher Royal Society of Chemistry
Language eng
Abstract Peptide-based biomaterials are key to the future of diagnostics and therapy, promoting applications such as tissue scaffolds and drug delivery vehicles. To realise the full potential of the peptide systems, control and optimisation of material properties are essential. Here we investigated the co-assembly of the minimal amyloid motif peptide, diphenylalanine (FF), and its tert-butoxycarbonyl (Boc)-modified derivative. Using Atomic Force Microscopy, we demonstrated that the co-assembled fibers are less rigid and show a curvier morphology. We propose that the Boc-modification of FF disrupts the hydrogen bond packing of adjacent N-termini, as supported by Fourier transform infrared and fluorescence spectroscopic data. Such rationally modified co-assemblies offer chemical functionality for after-assembly modification and controllable surface properties for tissue engineering scaffolds, along with tunable morphological vs. mechanical properties.
Formatted abstract
Peptide-based biomaterials are key to the future of diagnostics and therapy, promoting applications such as tissue scaffolds and drug delivery vehicles. To realise the full potential of the peptide systems, control and optimisation of material properties are essential. Here we investigated the co-assembly of the minimal amyloid motif peptide, diphenylalanine (FF), and its tert-butoxycarbonyl (Boc)-modified derivative. Using Atomic Force Microscopy, we demonstrated that the co-assembled fibers are less rigid and show a curvier morphology. We propose that the Boc-modification of FF disrupts the hydrogen bond packing of adjacent N-termini, as supported by Fourier transform infrared and fluorescence spectroscopic data. Such rationally modified co-assemblies offer chemical functionality for after-assembly modification and controllable surface properties for tissue engineering scaffolds, along with tunable morphological vs. mechanical properties.
Keyword Chemistry, Physical
Materials Science, Multidisciplinary
Physics, Multidisciplinary
Polymer Science
Chemistry
Materials Science
Physics
Polymer Science
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Chemical Engineering Publications
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Created: Mon, 09 Jan 2017, 20:18:56 EST by Noni Creasey on behalf of Learning and Research Services (UQ Library)