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.

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 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.

Citation

Creasey, R., Louzao, I., Arnon, Z., Marco, P., Adler-Abramovich, L., Roberts, C. J., Gazit, E., & Tendler, S. J. (2016). Disruption of diphenylalanine assembly by a Boc-modified variant. Soft Matter, 12(47), 9451-9457. https://doi.org/10.1039/c6sm01770c

• Journal Article Type: Article
• Acceptance Date: Nov 8, 2016
• Online Publication Date: Nov 8, 2016
• Publication Date: Nov 8, 2016
• Deposit Date: May 18, 2017
• Publicly Available Date: May 18, 2017
• Journal: Soft Matter
• Print ISSN: 1744-683X
• Electronic ISSN: 1744-6848
• Publisher: Royal Society of Chemistry
• Peer Reviewed: Peer Reviewed
• Volume: 12
• Issue: 47
• Pages: 9451-9457
• DOI: https://doi.org/10.1039/c6sm01770c
• Public URL: https://nottingham-repository.worktribe.com/output/829583
• Publisher URL: http://pubs.rsc.org/en/content/articlelanding/2016/sm/c6sm01770c#!divAbstract
• Additional Information: : This document is CrossCheck deposited; : Supplementary Information; : Rhiannon C. G. Creasey (ORCID); : Rhiannon C. G. Creasey (ResearcherID); : The Royal Society of Chemistry has an exclusive publication licence for this journal; : Received 2 August 2016; Accepted 8 November 2016; Accepted Manuscript published 8 November 2016; Advance Article published 14 November 2016; Version of Record published 28 November 2016
• Contract Date: May 18, 2017