(387ae) Instrument Development to Rapidly Screen Lyophilized Protein Stability

My PhD research addresses a critical bottleneck in biologics formulation: the multi-month timelines required for traditional lyophilized protein stability studies. I've developed novel optical instruments and solid-state spectroscopic techniques (low-frequency Raman and optical Kerr effect spectroscopy) that enable rapid, direct screening of excipients for long-term protein stability. This innovative approach has the potential to reduce formulation screening from several months to just minutes, significantly accelerating drug development and optimizing resource allocation for pharmaceutical companies.

Beyond instrument development, I have extensive experience in biophysical protein characterization, utilizing a range of techniques (e.g., DSC, DLS, CD, fluorescence spectroscopy, activity assays) to investigate protein stability, unfolding, and aggregation. This includes my work in elucidating the properties of a previously uncharacterized, stable protein intermediate of horseradish peroxidase. During this project, I mentored two undergraduate researchers, guiding their experimental design and data interpretation.

Research Interests: My anticipated PhD completion in October 2025 positions me to apply my strong background in instrument development, advanced analytical techniques, data interpretation, and innovative problem-solving to critical areas of formulation development, analytical R&D, or process analytical technology (PAT) within the pharmaceutical industry.