Hydrophobic dipeptide molecules have been induced to self-assemble into thin interfacial films at the air-water interface via drop-casting. The mechanism involves fiberlike strands, which exist in the high-pH spreading solvent, becoming intertwined at the surface of a low-pH subphase. Atomic force microscopy (AFM) reveals that the strands are similar to 40 nm wide and similar to 20 nm high and are woven together to form layers that can be up to similar to 800 nm thick. The use of Thioflavin T (ThT) fluorescence suggests that the dipeptides are ordered in a beta-sheet configuration irrespective of whether they form an interfacial film, while Fourier transform infrared spectroscopy (FTIR) shows the protonation effect for those which do form an interfacial film. The entanglement between protonated strands results in the formation of an elastic sheet. The interfacial films buckled under compression in a Langmuir trough and have the ability to convey long-term stability to large air bubbles.
- AMYLOID FIBRILS