Survival of the Brightest: The Effects of Environmental Stressors on Phycocyanin-Modeled Neo-Antigen Protein Stability

Overview

Globally, each year 20 million people are diagnosed with cancer. 61% of these people struggle with paying for expensive treatments like Neo-antigen therapies which cost $100,000, and CAR-T-cell therapy which costs over a million dollars. Furthermore, these immunotherapies work for only about 20% to 40% of patients. This means, in the majority of cases, the treatment does not lead to the desired remission. This is due to a variety of factors like storage conditions, protein-cell reactions, and problems with injecting the therapies. My project focuses on improving specifically storage conditions for Neo-antigen therapies to maximize therapeutic effectiveness and justify the cost. Neo-antigen proteins in mRNA-based cancer therapies must remain stable to be recognized by the immune system. If proteins destabilize, they cannot be identified. Protein stability is affected by temperature and pH. This project tested how these conditions affect protein stability using phycocyanin fluorescence as a model, which mimics neo-antigen behavior in immune recognition. I hypothesized fluorescence would remain stablest under cold, neutral conditions, critical for therapeutic function, and decay in warm or acidic environments. Five trials were conducted across nine conditions (acidic, neutral, basic at cold, room, and warm temperatures), with room-temperature water as the control. Fluorescence was measured every 15 minutes for two hours using a lux meter app. Lux values were averaged to calculate decay rate, % change, and fluorescence remaining to compare stability and brightness. Starting lux values ranged 11–25 and final values 7–19. Decay rates ranged 0.18–0.31% per minute, fluorescence remaining 61.02–77.77%, and % change 22.22–38.98%, with the control at 23.71%. Cold, neutral samples maintained higher fluorescence and lower decay rates, while warm, acidic samples showed greater loss. Temperature variability occurred, especially in warmer solutions. Colder, neutral conditions preserved fluorescence, and cold basic samples unexpectedly showed the slowest decay and highest fluorescence remaining, suggesting basic conditions can sustain proteins. Thermal quenching likely increased decay in warm solutions, while protonation reduced stability. Potential errors included uneven mixing and minor lighting fluctuations. Overall, the results mostly supported my hypothesis. These findings are significant for improving storage conditions to maximize therapeutic effectiveness. Future studies could test additional stressors like mechanical pressure, osmotic stress, and chemical agents.

Competition history

• CSEF 2026 Biochemistry/ Molecular Biology (Junior Division) · Entry J-04-09

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