(255ag) Self-Assembly of Di-Fmoc-L-Lysine Based Supramolecular Hydrogels

Rheology and nanostructure of supramolecular hydrogels formed by self-assembly of a peptide-based amphiphile, di-fluorenylmethyloxycarbonyl-lysine (di-Fmoc-L-lysine) will be presented. The hydrogels were prepared by dissolving the gelator in various solvents such as DMSO, DMF, acetone, methylene, ethanol, and propanol, followed by addition of water. The mechanical properties of these gels were investigated using shear and cavitation rheology. The gels display strain-softening behavior at moderate strain values. Structural analysis were conducted using FTIR, electron microscopy, and atomic force microscopy. Self-assembled fibers with lateral dimensions ranging from 10 to 50 nm were captured in microscopy studies. FTIR results indicate β-sheet-like conformation of the peptides in the hydrogel.