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

Meghan Hughes, Pim W. J. M. Frederix, Jaclyn Raeburn, Louise S. Birchall, Jan Sadownik, Fiona C. Coomer, I-Hsin Lin, Edmund J. Cussen, Neil T. Hunt, Tell Tuttle, Simon J. Webb, Dave J. Adams, Rein V. Ulijn

Research output: Contribution to journalArticlepeer-review

83 Citations (Scopus)

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 beta-sheets which interlock via pi-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.

Original languageEnglish
Pages (from-to)5595-5602
Number of pages8
JournalSoft Matter
Volume8
Issue number20
DOIs
Publication statusPublished - 2012

Keywords

  • peptide derivatives
  • supramolecular structures
  • spectroscopy
  • infrared spectroscopy
  • X-ray diffraction analysis

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