Abstract
Tuning structures: Stimulus-responsive peptide self-assembly requires a balance of conformational change and structural continuity of stable β sheets. In an amphiphilic bipyridine–tripeptide model, temperature, and ultrasound switch a reversible morphological transformation between vesicles and nanofibers (see picture) through the synergistic effects of terminal β-sheet-forming peptides, flexible linkers, and rotatable bipyridine groups.
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