Picture of virus under microscope

Research under the microscope...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

Explore SIPBS research

Biocatalytic self-assembly of 2D peptide-based nanostructures

Hughes, M. and Xu, haixia and Frederix, Pim and Smith, A.M. and Hunt, Neil and Tuttle, Tell and Kinloch, I.A. and Ulijn, Rein Vincent (2011) Biocatalytic self-assembly of 2D peptide-based nanostructures. Soft Matter, 7 (21). pp. 10032-10038. ISSN 1744-683X

Full text not available in this repository. (Request a copy from the Strathclyde author)

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 nanostructures via 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.