Supramolecular hydrogels are expected to have applications as novel soft materials in various fields owing to their designable functional properties. Herein, we developed an in situ synthesis of supramolecular hydrogelators, which can trigger gelation of an aqueous solution without the need for temperature change. This was achieved by mixing two precursors, which induced the synthesis of a supramolecular gelator and its instantaneous self-assembly into nanofibers. We then performed the in situ synthesis of this supramolecular gelator at an oil/water interface to produce nanofibers that covered the surfaces of the oil droplets (nanofiber-stabilized oil droplets). External stimuli induced fusion of the droplets owing to disassembly of the gelator molecules. Finally, we demonstrated that this stimuli-induced droplet fusion triggered a synthetic reaction within the droplets. This means that the confined nanofiber-stabilized droplets can be utilized as stimuli-responsive microreactors.

Supramolecular hydrogels are expected to have applications as novel soft materials in various fields owingt o their designable functional properties.Herein, we developed an in situ synthesis of supramolecular hydrogelators,w hich can trigger gelation of an aqueous solution without the need for temperature change.T his was achieved by mixing two precursors,w hichi nduced the synthesis of as upramolecular gelator and its instantaneous self-assembly into nanofibers.W e then performed the in situ synthesis of this supramolecular gelator at an oil/water interface to produce nanofibers that covered the surfaces of the oil droplets (nanofiber-stabilized oil droplets). External stimuli induced fusion of the droplets owing to disassembly of the gelator molecules.F inally,w ed emonstrated that this stimuli-induced droplet fusion triggered as ynthetic reaction within the droplets.T his means that the confined nanofiber-stabilized droplets can be utilized as stimuli-responsive microreactors.

We investigated D-amino acids as potential inhibitors targeting L-peptide toxins. Among the L-and D-amino acids tested, we found that D-tryptophan (D-Trp) acted as an inhibitor of melittin-induced hemolysis. We then evaluated various Trp derivatives and found that 5-chlorotryptamine (5CT) had the largest inhibitory effect on melittin. The indole ring, amino group, and steric hindrance of an inhibitor played important roles in the inhibition of melittin activity. Despite the small size and simple molecular structure of 5CT, its IC 50 was approximately 13 μg/mL. Fluorescence quenching, circular dichroism measurements, and size-exclusion chromatography revealed that 5CT interacted with Trp19 in melittin and affected the formation of the melittin tetramer involved in hemolysis. Molecular dynamics simulation of melittin also indicated that the interaction of 5CT with Trp19 in melittin affected the formation of the tetramer.

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