Vitrification.
We engineer intrinsically disordered proteins, modeled on tardigrade CAHS families, that form protective glass matrices around sensitive biomolecules — replacing the cold chain with chemistry.
Three pillars: the molecular mechanisms of cryptobiosis, their translation into medicine, and the controlled return from suspended states.
We engineer intrinsically disordered proteins, modeled on tardigrade CAHS families, that form protective glass matrices around sensitive biomolecules — replacing the cold chain with chemistry.
Our preservation platforms extend the shelf life of vaccines and biologics from months to years at ambient temperature, with the goal of reaching the regions cold storage cannot.
We investigate the controlled return from suspended states — the precise conditions under which paused biological systems resume function without loss.
We use machine learning to search the space of disordered proteins, cryoprotectants, and drying protocols — predicting which molecular combinations will vitrify, which will fail, and which have never been tried.