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Minimal Tripeptides Enable Refrigeration-Free Stabilization of Vaccines and Proteins

It offers a refrigeration-free platform to protect vaccines through a nature-inspired peptide phase-separation process.

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Overview

  • CUNY ASRC team led by Rein Ulijn and Ye He showed that simple three-amino-acid peptides undergo liquid–liquid phase separation during drying to form porous assemblies that encapsulate and protect proteins.
  • Electron microscopy and rehydration tests confirmed that these reversible microparticles release proteins intact after stress-induced dehydration.
  • The approach draws on tardigrade desiccation strategies to replicate natural stress-response compartments without complex formulations.
  • Published August 5 in Nature Materials, the study highlights prospects for stabilizing vaccines and therapeutic proteins without cold-chain logistics.
  • Supported by the Air Force Office of Scientific Research with collaborators at City College of New York, Hunter College and Columbia University, the team is now exploring practical applications in vaccine distribution and responsive materials.