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Issue 21, 2011
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Biocatalytic self-assembly of 2D peptide-based nanostructures

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Abstract

Peptide based 2D nanostructures of micronscale size in both X and Y dimensions are extremely rare because amino acid chirality favours helical structures, and nucleation-growth mechanisms usually favour uni-directional growth. We demonstrate the production of extended two-dimensional (2D) peptide nanostructuresvia the thermolysin catalysed condensation of Fmoc protected hydrophilic amino acid (serine, Fmoc-S) and a hydrophobic amino acid ester (phenylalanine, F-OMe). We propose that lateral self-assembly is enabled by the reversible nature of the system, favouring the thermodynamic product (extended sheets) over kinetically favoured 1 dimensional structures. Fmoc-SF-OMe forms extended arrays of β-sheet structures interlock via π-stacking between Fmoc groups. We propose that, due to its alternating hydrophilic/hydrophobic amino acid sequence, amphiphilic sheets presenting either phenyl or hydroxyl functionality are formed that assemble pair-wise, thereby shielding hydrophobic groups from the aqueous environment. Formation of these structures was supported by fluorescence emission spectroscopy, FTIR and XRD analysis and molecular mechanics minimization. At enhanced enzyme concentrations, hierarchical self-assembly was observed giving rise to spherulitic structures, with the number of spherulites dictated by enzyme concentration.

Graphical abstract: Biocatalytic self-assembly of 2D peptide-based nanostructures

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Publication details

The article was received on 27 May 2011, accepted on 16 Aug 2011 and first published on 06 Sep 2011


Article type: Paper
DOI: 10.1039/C1SM05981E
Citation: Soft Matter, 2011,7, 10032-10038
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    Biocatalytic self-assembly of 2D peptide-based nanostructures

    M. Hughes, H. Xu, P. W. J. M. Frederix, A. M. Smith, N. T. Hunt, T. Tuttle, I. A. Kinloch and R. V. Ulijn, Soft Matter, 2011, 7, 10032
    DOI: 10.1039/C1SM05981E

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