A vaccine can be scientifically perfect and still fail to reach the person who needs it. Sometimes the problem is a refrigerator. We design proteins that keep biologics alive without one.
The cold chain is the network of refrigerated storage and transport that keeps biologics usable from manufacturer to patient. Where reliable electricity is hard to maintain, that network becomes the thing standing between a working intervention and the person who needs it.
Preserving biologics without freezing is already possible. Trehalose, a sugar widely used for stabilisation, protects molecules during drying. But protection during drying is not protection during storage in a hot, humid clinic. Spray-dried trehalose can fail outright when the sugar crystallises in humidity and releases the cargo it was protecting.
That distinction is the whole point. The question is not whether we can dry a biologic. It is whether we can make one survive the journey.
SCHEMATIC — NOT DATA. Illustrates the two published storage outcomes described above. No Wyrd Bio results exist yet.
Dried bacteriophage held at 25 °C over a few months.
Enzyme protection by natural tardigrade CAHS proteins, in published work.
Published work uses natural CAHS or small point mutations. Nothing built from the principle up.
Tardigrades survive extreme dehydration partly through intrinsically disordered proteins called CAHS. Instead of folding into a rigid structure, these proteins change as water disappears, vitrifying into glass-like states that physically stabilise fragile molecules.
A 2023 study ruled out the earlier idea that they work by retaining water. The mechanism looks closer to encasement than hydration — the cargo is held still rather than kept wet.
This is not speculative. Natural CAHS proteins have protected enzymes about an order of magnitude better than trehalose, stabilised human clotting Factor VIII in a dry state, and helped preserve engineered bacteria and synthetic cells.
The tun is the desiccated form. Metabolism stops; CAHS proteins vitrify around what must be preserved. Our work takes the physics of that inner state and leaves the animal behind.
Evolution shaped CAHS for a tardigrade’s survival, not for keeping a vaccine alive in a humid clinic. We build to the physical principle instead of copying the artefact — then test it where current methods actually break.
Generate candidate sequences with open computational tools, guided by the properties associated with CAHS protection: intrinsic disorder, charge distribution, and behaviour during drying. Filter computationally, carry the best two or three forward.
Express the selected genes in E. coli under laboratory supervision. CAHS-type proteins are heat-soluble, so purification can often be done by boiling the lysate and keeping the soluble fraction — no expensive chromatography required.
Combine each candidate with a model cargo, dry under controlled conditions, then hold at elevated temperature and humidity for defined periods. Primary readout is how much biological activity survives. Every arm runs head-to-head, with controls built in from the start.
These came out of how the first project was designed, not from a values exercise.
Where we can state the physical principle behind something, we build to the principle. Slower, more likely to fail, and the only route to something genuinely new.
Not where they look good. We run experiments under the conditions that cause failure in the field, even when that makes our own results worse.
Every claim runs head-to-head against what people already use. If trehalose wins, we report that trehalose wins.
An experiment designed so failure is informative beats one designed so success is likely. We publish the answer we get.
Especially interested in hearing from labs in and around Hyderabad with a plate reader and bench space, and from anyone who thinks this will not work.
hello@wyrd.bio