Disruption of diphenylalanine assembly by a Boc-modified variant
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 invesigated the co-ass...
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| Format: | Article |
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Royal Society of Chemistry
2016
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| Online Access: | https://eprints.nottingham.ac.uk/42919/ |
| _version_ | 1848796601980551168 |
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| author | Creasey, Rhiannon Louzao, Iria Arnon, Zohar Marco, Pini Adler-Abramovich, Lihi Roberts, Clive J. Gazit, Ehud Tendler, Saul J.B. |
| author_facet | Creasey, Rhiannon Louzao, Iria Arnon, Zohar Marco, Pini Adler-Abramovich, Lihi Roberts, Clive J. Gazit, Ehud Tendler, Saul J.B. |
| author_sort | Creasey, Rhiannon |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | 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 invesigated 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. |
| first_indexed | 2025-11-14T19:50:35Z |
| format | Article |
| id | nottingham-42919 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T19:50:35Z |
| publishDate | 2016 |
| publisher | Royal Society of Chemistry |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-429192020-05-04T18:21:56Z https://eprints.nottingham.ac.uk/42919/ Disruption of diphenylalanine assembly by a Boc-modified variant Creasey, Rhiannon Louzao, Iria Arnon, Zohar Marco, Pini Adler-Abramovich, Lihi Roberts, Clive J. Gazit, Ehud Tendler, Saul J.B. 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 invesigated 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. Royal Society of Chemistry 2016-11-08 Article PeerReviewed Creasey, Rhiannon, Louzao, Iria, Arnon, Zohar, 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). pp. 9451-9457. ISSN 1744-6848 http://pubs.rsc.org/en/content/articlelanding/2016/sm/c6sm01770c#!divAbstract doi:10.1039/C6SM01770C doi:10.1039/C6SM01770C |
| spellingShingle | Creasey, Rhiannon Louzao, Iria Arnon, Zohar Marco, Pini Adler-Abramovich, Lihi Roberts, Clive J. Gazit, Ehud Tendler, Saul J.B. Disruption of diphenylalanine assembly by a Boc-modified variant |
| title | Disruption of diphenylalanine assembly by a Boc-modified variant |
| title_full | Disruption of diphenylalanine assembly by a Boc-modified variant |
| title_fullStr | Disruption of diphenylalanine assembly by a Boc-modified variant |
| title_full_unstemmed | Disruption of diphenylalanine assembly by a Boc-modified variant |
| title_short | Disruption of diphenylalanine assembly by a Boc-modified variant |
| title_sort | disruption of diphenylalanine assembly by a boc-modified variant |
| url | https://eprints.nottingham.ac.uk/42919/ https://eprints.nottingham.ac.uk/42919/ https://eprints.nottingham.ac.uk/42919/ |