Divergent self-assembly propensity of enantiomeric phenylalanine amphiphiles that undergo pH-induced nanofiber-to-nanoglobule conversion.

This study presents the pathway diversity in the self-assembly of enantiomeric single phenylalanine derived amphiphiles (single F-PDAs), L-NapF-EDA and D-NapF-EDA, that form supramolecular hydrogels at varied concentrations (≥1 mg mL and ≥3 mg mL, respectively). By fitting the variable temperature circular dichroism (VT-CD) data to the isodesmic model, various thermodynamic parameters associated with their self-assembly, such as association constant (), changes in enthalpy (Δ), entropy (Δ), and Gibbs free energy (Δ), were extracted. The self-assembly of these single F-PDAs was found to be enthalpy-driven but entropically-disfavored.