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Nature Materials | Volume 24 | September 2025 | 1465–1475 1465nature materialshttps://doi.org/10.1038/s41563-025-02300-z ArticleAdaptive peptide dispersions enable drying-induced biomolecule encapsulation Dhwanit R. Dave    1,2,3,14 , Salma Kassem 1,14 , Maeva Coste    1,14 , Lele Xu    1,4,14 , Mona Tayarani-Najjaran    1,2,3,14 , Darjan Podbevšek    1,5 , Paola Colon-De Leon    1,2,3 , Sheng Zhang    1 , Luis Ortuno Macias    5 , Deborah Sementa    1 , María Pérez-Ferreiro    1,6 , Nooshin Sadat Ayati    5 , Muniyat A. Choudhury 1,7 , Kelly Veerasammy 1 , Selma Doganata 1,7 , Tiffany Zhong    8 , Cory Weng 1,7 , Jorge Morales 9 , Denize C. Favaro    1 , Mateusz Marianski    2,3,10 , So Yeon Ahn    11 , Allie C. Obermeyer    11 , Tong Wang    1 , Tai-De Li    1,12 , Xi Chen    1,2,5,13 , Raymond Tu    5 , Ye He    1,4,9 & Rein V. Ulijn    1,2,3,10 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 fl exible 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 solidif i cation, resulting in the formation of fi lms of stif f , 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 ef f i cient encapsulation and the retention of protein stability after redispersion, showing promise for the emulsif i cation, encapsulation, protection and storage o f b io ma cromolecules. The mechanism resembles the protective strategies in natural systems during desiccation, which rely on liquid–liquid phase separation to survive extreme conditions.All life forms share conserved sets of building blocks. Biomolecular covalent and non-covalent interactions dictate the rich structural design space, supporting wide-ranging functions, including recogni-tion, self-assembly, catalysis and shapeshifting. Beyond their critical roles in the chemistry of life, these structures provide inspiration for supramolecular materials 1–4 and systems 5 for various technological and biotechnological applications 6–8 .Peptide materials usually contain patterns of backbone hydrogen bonding derived from protein secondary structures 9–13 , typically giv-ing rise to ordered one-dimensional (1D) 14 , two-dimensional (2D) 15,16 or three-dimensional (3D) 17 assemblies. These hydrogen-bond patterns may be further stabilized by aromatic stacking 18,19 , giving rise to archi-tectures that are remarkably stiff and stable 20 . This is exemplified by ‘dry’ diphenylalanine (FF) zippers 21 , where the chiral organization of side chains provides additional control over assembly structures 22 . We previously established that aromatic tripeptides with polar groups, such as lysine–tyrosine–phenylalanine (KYF), retain strong directional self-assembly tendencies complemented with favourable solvent interactions, leading to hydrogelation 23 .Besides ordered structures, the notion of non-directional assem-bly is also common in biology, for example, in liquid condensates, where it typically leads to spherical morphologies dictated by surface Received: 24 October 2023Accepted: 24 June 2025Published online: 5 August 2025 Check for updatesA full list of affiliations appears at the end of the paper.  e-mail: yhe1@gc.cuny.edu; rulijn@gc.cuny.edu