Adaptive peptide dispersions enable drying-induced biomolecule encapsulation

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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Publication Details

Journal
Nature Materials
Published
2025-08-05
DOI
https://doi.org/10.1038/s41563-025-02300-z
Citations
8
Primary Topic
Supramolecular Self-Assembly in Materials
Type
article
Field-Weighted Citation Impact
4.78

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article

Adaptive peptide dispersions enable drying-induced biomolecule encapsulation

Ye He, Sheng Zhang, Mateusz Marianski, Jorge Morales et al.
8 citations
Nature Materials
Supramolecular Self-Assembly in Materials
4.78
article

Adaptive peptide dispersions enable drying-induced biomolecule encapsulation

Ye He, Sheng Zhang, Mateusz Marianski, Jorge Morales, Tiffany Zhong, Darjan Podbevšek, Rein V. Ulijn, Salma Kassem, Dhwanit Dave, Nooshin Sadat Ayati, Deborah Sementa, Mona Tayarani-Najjaran, Allie C. Obermeyer, Muniyat A. Choudhury, Tai‐De Li, Denize C. Favaro, Raymond S. Tu, Maëva Coste, Cory Weng, Kelly Veerasammy, So Yeon Ahn, María Pérez-Ferreiro, Selma Doganata, Luis E. Ortuno Macias, Xi Chen, Tong Wang, Lele Xu, Pablo de León
article en
8 citations

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.

Nature MaterialsVol. 24(9)
Universidade da Coruña (ES), The Graduate Center, CUNY (US), City College of New York (US), City University of New York (US), Princeton University (US), Hunter College (US), CUNY Advanced Science Research Center (US), Columbia University (US)
National Science Foundation, Alfred P. Sloan Foundation, City University of New York, Advanced Storage Research Consortium, National Institutes of Health, Office of Naval Research, Core Research for Evolutional Science and Technology
Openalex Percentile: Top 5%
Supramolecular Self-Assembly in Materials
4.78
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