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Abstract
Self-assembled supramolecular structures of peptide derivatives often reflect a kinetically trapped state rather than the thermodynamically most favoured structure, which presents a challenge when trying to elucidate the molecular design rules for these systems. In this article we use thermodynamically controlled self-assembly, driven by enzymatic condensation of amino acid derivatives, to elucidate chemical composition/nanostructure relationships for four closely related Fmoc-dipeptide-methyl esters which form hydrogels; SF, SL, TF and TL. We demonstrate that each of the four systems self-assemble to form extended arrays of beta-sheets which interlock via pi-stacking of Fmoc-moieties, yet with subtle differences in molecular organisation as supported by rheology, fluorescence emission spectroscopy, infrared spectroscopy, X-ray diffraction analysis and molecular mechanics minimisation.
Original language | English |
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Pages (from-to) | 5595-5602 |
Number of pages | 8 |
Journal | Soft Matter |
Volume | 8 |
Issue number | 20 |
DOIs | |
Publication status | Published - 2012 |
Keywords
- peptide derivatives
- supramolecular structures
- spectroscopy
- infrared spectroscopy
- X-ray diffraction analysis
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Dive into the research topics of 'Sequence/structure relationships in aromatic dipeptide hydrogels formed under thermodynamic control by enzyme-assisted self-assembly'. Together they form a unique fingerprint.Projects
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Equipment
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Computational Insights into Peptide Self-Assembly
Tell Tuttle (Invited speaker)
19 Nov 2013Activity: Talk or presentation types › Invited talk
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Fibrous Protein Nanocomposites for Tailored Hybrid Biostructures and Devices
Tell Tuttle (Invited speaker)
9 Oct 2012Activity: Participating in or organising an event types › Participation in conference
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238th ACS National Meeting
Tell Tuttle (Speaker)
23 Aug 2012Activity: Participating in or organising an event types › Participation in conference