ArticleNature materials2025
Adaptive peptide dispersions enable drying-induced biomolecule encapsulation.
Article in Nature materials, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Backbone Hydrogen Bonding as a Determinant of Condensate Material States.Journal of the American Chemical Society · 2026Article
- Programmable Multiphasic Condensates Formed via Evaporation-Induced Phase Separation of Minimal Peptide Model.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Lipoengineering of Biomolecular Condensates Controls Material Properties and Multiphase Hierarchy to Guide Organoid Morphogenesis.bioRxiv : the preprint server for biology · 2026Article
- Nanoparticulate protectants for the dry storage of protein therapeutics.Nanomedicine (London, England) · 2026Review
- From biomolecular condensates to functional nanomaterials: LLPS-inspired frameworks for nanoscale hydrogels and adaptive materials.Journal of nanobiotechnology · 2026Review
- Liquid-liquid phase separation of peptides: a molecular foundation for next-generation biomaterials.Chemical science · 2026Review
- Intrinsically Disordered Protein Coating for Oral Delivery of Peptide Drugs.bioRxiv : the preprint server for biology · 2025Article
- Tripeptide armour shields encapsulated proteins.Nature materials · 2025Article
Corrections and comments
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Authors and funding
28 authors.
Funding
Abstract
Peptides are promising building blocks of designer materials with wide-ranging applications. These materials are stabilized by directional hydrogen-bonding patterns, giving rise to one-dimensional 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 highly soluble dynamic ensembles through multivalent side-chain interactions. We observe these supramolecular dispersions undergo drying-induced sequential liquid-liquid phase separation followed by solidification, resulting in the formation of films of stiff, densely packed and porous peptide microparticles that can be instantaneously redispersed upon the re-introduction of water. Air-drying of peptide dispersions in the presence of proteins or small-molecule payloads results in efficient encapsulation and the retention of protein stability after redispersion, showing promise for the emulsification, encapsulation, protection and storage of biomacromolecules. The mechanism resembles the protective strategies in natural systems during desiccation, which rely on liquid-liquid phase separation to survive extreme conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.