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Issue 20, 2012
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Sequence/structure relationships in aromatic dipeptide hydrogels formed under thermodynamic control by enzyme-assisted self-assembly

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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 β-sheets which interlock via π-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.

Graphical abstract: Sequence/structure relationships in aromatic dipeptide hydrogels formed under thermodynamic control by enzyme-assisted self-assembly

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Publication details

The article was received on 30 Jan 2012, accepted on 19 Mar 2012 and first published on 13 Apr 2012


Article type: Paper
DOI: 10.1039/C2SM25224D
Citation: Soft Matter, 2012,8, 5595-5602
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    Sequence/structure relationships in aromatic dipeptide hydrogels formed under thermodynamic control by enzyme-assisted self-assembly

    M. Hughes, P. W. J. M. Frederix, J. Raeburn, L. S. Birchall, J. Sadownik, F. C. Coomer, I. Lin, E. J. Cussen, N. T. Hunt, T. Tuttle, S. J. Webb, D. J. Adams and R. V. Ulijn, Soft Matter, 2012, 8, 5595
    DOI: 10.1039/C2SM25224D

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