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

Hughes, M. et al. (2012) Sequence/structure relationships in aromatic dipeptide hydrogels formed under thermodynamic control by enzyme-assisted self-assembly. Soft Matter, 8(20), pp. 5595-5602. (doi: 10.1039/C2SM25224D)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Adams, Dave
Authors: Hughes, M., Frederix, P. W. J. M., Raeburn, J., Birchall, L. S., Sadownik, J., Coomer, F. C., Lin, I.-H., Cussen, E. J., Hunt, N. T., Tuttle, T., Webb, S. J., Adams, D. J., and Ulijn, R. V.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Soft Matter
Publisher:Royal Society of Chemistry
ISSN:1744-683X
ISSN (Online):1744-6848
Published Online:13 April 2012

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