The Bright Side of Biologic Stability: A Thermofluor Screen for Rational Buffer Optimization 

By Jacob Poxon and Jordan Potts, Upperton Pharma Solutions

Therapeutic proteins, such as monoclonal antibodies (mAbs), are increasingly used in injectable formulations to treat a wide range of conditions. However, their complex structures make them particularly vulnerable to denaturation, aggregation, and chemical degradation. These are issues that can compromise safety and drug efficacy. 

Formulating injectable buffers that stabilize these biologics is critical but challenging. Injectable buffers work to stabilize proteins by enhancing non-covalent interactions. Thus, protecting against environmental factors, and minimizing chemical instabilities such as oxidation, reduction and deamidation. Traditional methods for buffer screening (e.g., buffer exchange and circular dichroism) are often low-throughput, time-consuming, and resource-intensive.

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