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 language | English |
---|---|
Pages (from-to) | 5595-5602 |
Number of pages | 8 |
Journal | Soft Matter |
Volume | 8 |
Issue number | 20 |
DOIs | |
Publication status | Published - 2012 |
Externally published | Yes |
Keywords
- SUPRAMOLECULAR HYDROGELS
- NANOPARTICLE ARRAYS
- MOLECULAR-DYNAMICS
- NANOSTRUCTURES
- ORGANIZATION
- ARCHITECTURE
- NANOFIBERS
- NANOTUBES
- PEPTIDES
- PROTEINS