作者
Rhiannon CG Creasey, Iria Louzao, Zohar A Arnon, Pini Marco, Lihi Adler-Abramovich, Clive J Roberts, Ehud Gazit, Saul JB Tendler
发表日期
2016
期刊
Soft Matter
卷号
12
期号
47
页码范围
9451-9457
出版商
Royal Society of Chemistry
简介
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 …
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RCG Creasey, I Louzao, ZA Arnon, P Marco… - Soft Matter, 2016