ers properties; they make water a liquid at room temperature. All biological fluids, which are composed mostly of water, are also defined by their hydrogen bonds. Without these bonds, proteins would unfold, and life as we know it would be impossible. Sugars used to safeguard protein-based drugs act like cement, taking the place of water by bonding to the proteins and locking them in place. By rapidly freezing liquid sugar, its molecules have no time to form the usual orderly crystal patterns typically found in sugars that are solids at room temperature. Lead NIST researcher Marc Cicerone says that the randomly ordered sugar molecules fit the encased proteins like a glove, stiffening molecular motions that cause the proteins to chemically degrade.
Using the fluorescent probe, the team can now tell within minutes after freeze-drying the protein whether the formulation will be stable, reducing the time and expense associated with the wait and see method currently in use.
Instead of needing relaxation measurements that require using neutron scatteringa national facility with limited time availabilitywe have developed a widely accessible solution in the form of readily available steady-state fluorescence measurements, Cicerone says. This will allow pharmaceutical companies to adopt the new metrology weve developed.
When applied, the teams findings should help to increase the availability of viable medicines in places where refrigeration is scarce or unavailable.
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