Biocatalytic self-assembly of 2D peptide-based nanostructures

M. Hughes, haixia Xu, Pim Frederix, A.M. Smith, Neil Hunt, Tell Tuttle, I.A. Kinloch, Rein Vincent Ulijn

Research output: Contribution to journalArticlepeer-review

58 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)10032-10038
Number of pages7
JournalSoft Matter
Issue number21
Early online date6 Sept 2011
Publication statusPublished - 2011


  • peptide-based nanostructures
  • nanostructures
  • spherulites
  • TIC - Bionanotechnology


Dive into the research topics of 'Biocatalytic self-assembly of 2D peptide-based nanostructures'. Together they form a unique fingerprint.

Cite this