A groundbreaking discovery from researchers at Penn State University promises to revolutionize how protein-based drugs and vaccines are stored and distributed. For decades, biologic drugs—such as insulin, monoclonal antibodies, and viral vaccines—have relied on refrigeration to maintain their stability and effectiveness. However, a new method developed by Penn State researchers eliminates the need for cold storage, potentially transforming the accessibility, affordability, and distribution of these life-saving medicines.
Currently, over 80% of biologic drugs and 90% of vaccines require strict temperature-controlled conditions to maintain their effectiveness. Scott Medina, the study’s lead author and William and Wendy Korb Early Career Professor of Biomedical Engineering at Penn State, explains that this cold-chain requirement places significant constraints on the global distribution of essential healthcare products. “This approach could revolutionize their storage and distribution, making them more accessible and affordable for everyone,” he said. The research, published in Nature Communications, holds the potential to save billions of dollars currently spent on refrigeration and enable the use of protein-based therapies in settings where constant refrigeration is not possible, such as remote or conflict-stricken regions.
The Challenge of Storing Protein-Based Drugs
Protein-based drugs and vaccines, such as those used for treating diabetes (insulin), certain cancers (monoclonal antibodies), and viral infections (vaccines), are fragile and highly sensitive to environmental conditions, particularly heat, light, and movement. These products rely on a delicate balance to preserve their biological activity—if exposed to improper temperatures, the proteins they contain can degrade, leading to ineffectiveness and the potential for harm.
Typically, these biological products are stored in refrigeration units ranging from 36 to 46°F, slowing down the natural process of protein degradation. However, freezing and refrigeration introduce additional complications such as logistics, energy consumption, and the risk of product damage or loss during transportation. These challenges are especially pronounced in regions with limited access to refrigeration facilities, adding extra barriers to healthcare access in underserved communities.
Breakthrough: Oil-Based Solution for Protein Stabilization
The new method developed by the Penn State researchers substitutes the water-based solution traditionally used for protein storage with a unique perfluorocarbon oil-based solution. Perfluorocarbons are stable, non-toxic oils that have previously been used in other biomedical applications, including blood substitutes. These oils are chemically inert and are highly effective in storing proteins without disrupting their structural integrity, even under stressful environmental conditions like heat.
To test this novel oil-based solution, the team experimented with five different proteins—each serving a different health-related function, such as antibodies and enzymes. These proteins are typically used to treat various diseases, including cancers, infectious diseases, and metabolic disorders. The team found that these proteins maintained their efficacy and were able to perform their desired functions when tested in live animal models, without any noticeable toxicity or adverse health effects.
“The new solution was just as effective as the refrigerated versions, and the proteins performed their jobs in the mice without any signs of toxicity,” said Medina. Another major benefit of this oil-based storage solution is its natural sterility. Bacteria, fungi, and viruses, which thrive in water-based environments, cannot grow or contaminate the protein samples stored in perfluorocarbons. This sterility is a critical feature that ensures that the stored products are safe for use and have a longer shelf life, even without refrigeration.
The Science Behind the Surfactant
Despite the promise of perfluorocarbon oils, proteins traditionally perform poorly in oil solutions because they do not readily dissolve in oil. This presents a significant challenge for ensuring that the proteins remain stable and evenly dispersed in the solution. However, the researchers overcame this problem by introducing a key innovation: the development of a surfactant molecule.
A surfactant is a molecule with hydrophilic (water-attracting) and hydrophobic (water-repelling) parts. The Penn State research team used the surfactant to coat the surface of the protein molecules. The hydrophilic component of the surfactant binds with the protein, while the hydrophobic part interacts with the oil. This coating allowed the proteins to disperse evenly throughout the oil solution and effectively stabilized the proteins against heat, degradation, and contamination.
“Think of it like raincoats for proteins,” Medina explained. “Just like a raincoat keeps you dry, this protective shell keeps the protein safe from heat and contamination, allowing it to stay stable and functional.” The protective surfactant layer essentially shields the proteins from environmental factors that would normally cause them to break down, such as temperature fluctuations and microbial contamination.
Resilience to Heat and Environmental Stressors
Proteins are particularly vulnerable to the destabilizing effects of heat. Under normal conditions, when proteins are exposed to high temperatures, their molecules vibrate and unfold, losing their functional three-dimensional structure. Without this specific structural arrangement, proteins become inactive, leading to the degradation of their therapeutic properties. Through their experiments, the researchers demonstrated that by encapsulating proteins in the surfactant-protected oil-based solution, the proteins retained their functional shape, even at temperatures as high as 212°F (100°C)—far beyond what is required to boil water.
This thermal stability is one of the most remarkable aspects of the Penn State team’s innovation. Not only can the proteins survive extreme temperatures, but they also remain functional, preserving their original therapeutic abilities. The surfactant effectively shields the proteins from the energetic forces that would otherwise cause them to unfold, allowing these essential medicines to remain viable under challenging environmental conditions.
Implications for Drug and Vaccine Distribution
The impact of this research cannot be overstated. The global healthcare industry faces ongoing challenges related to cold-chain logistics. In 2020, researchers projected that the cost of cold chain logistics would reach $58 billion globally by 2026. A substantial portion of these costs stems from transporting temperature-sensitive drugs and vaccines under controlled conditions. Inadequate refrigeration during transit can lead to the loss of precious and costly biological products, especially in regions with insufficient infrastructure or during emergencies.
Medina highlights that one of the most significant outcomes of this research is the potential to eliminate the cold chain altogether. “This new method could also lower barriers and allow the drugs to be distributed in resource-scarce environments across all populations,” Medina explained. Whether it’s rural areas with limited access to healthcare, natural disaster zones, or military combat zones where refrigeration units are impractical, this discovery could ensure that protein-based therapies are available to people who need them the most.
In terms of cost savings, removing the refrigeration requirement can have a profound financial impact. Pharmaceutical companies can reduce the costs associated with storing, packaging, and distributing temperature-sensitive biologics, leading to lower prices for patients and governments. These savings could also encourage manufacturers to make life-saving therapies more widely available, particularly in underserved regions that previously lacked reliable access to temperature-controlled supply chains.
A Step Forward: Future Directions
The Penn State researchers, led by Medina, plan to build on this work by testing additional proteins and peptides that could be stabilized using this novel technique. Their goal is to partner with pharmaceutical companies and continue refining the process for commercialization. As Medina noted, the team is currently working on securing patent rights and exploring how they can help pharmaceutical companies stabilize protein molecules or peptides, paving the way for widespread use in numerous medical treatments.
“In the future, we hope to demonstrate that our method can work with a broader range of proteins and medications. Partnering with pharmaceutical companies is key to applying our work to the real world and improving patient outcomes,” Medina said.
The broader implications of this innovation are extraordinary: beyond cost savings and logistical improvements, this discovery has the potential to transform global healthcare delivery by improving the availability of essential biologic medicines. It could help ensure that people, no matter where they live, have access to the medications they need to stay healthy and fight diseases.
Conclusion
The discovery of an oil-based storage solution for protein-based drugs and vaccines marks a transformative shift in biomedicine. By replacing traditional water-based solutions with a perfluorocarbon oil solution, this breakthrough approach eliminates the need for refrigeration, making vital biologics more accessible, stable, and cost-effective for global distribution. This research offers not only potential cost savings but also new hope for improving healthcare in resource-limited settings and conflict zones, where access to refrigeration is often a significant barrier.
As the technology continues to develop, we can anticipate a future where protein therapies are no longer tied to strict cold-chain logistics but can be stored, shipped, and distributed with greater ease and efficiency, ultimately improving access to life-saving treatments for millions of people worldwide.
Reference: Atip Lawanprasert et al, Heat stable and intrinsically sterile liquid protein formulations, Nature Communications (2024). DOI: 10.1038/s41467-024-55304-9