Adaptive and Space-Filling Peptide Self-Assembly Upon Drying

Peptides have tremendous potential as building blocks of designer materials with wide-ranging applications. These materials are stabilized by strongly directional hydrogen bonding patterns giving rise to one-, or two-dimensional assembly. It remains a challenge to mimic biology’s context-adaptive and flexible structures. Here, we introduce minimalistic tripeptide sequences that form dynamic ensembles through incorporation of multivalent sidechain interactions that collectively self-optimize depending on their context. Notably, we observed that these dispersions undergo drying-induced liquid to solid phase separation involving interface stabilization and expansion, resulting in formation of films of stiff, and densely packed, porous peptide microparticles that can be instantaneously redispersed upon re-introduction of water. Air-drying of aqueous peptide dispersions in the presence of proteins or small molecule payloads results in spontaneous and efficient encapsulation, and retention of protein stability after redispersion. These supramolecular tripeptide dispersions show promise for emulsification, encapsulation, and storage of biomacromolecules.