Rational engineering strategies for enhancing antibody fragment utility
Abstract: Therapeutic antibodies have become one of the most widely used classes of biotherapeutics due to their unique antigen specificity and their ability to be engineered against diverse disease targets. There is significant interest in utilizing truncated antibody fragments, including nanobodies, as therapeutics, as their small size affords favorable properties such as increased tumor penetration as well as the ability to utilize lower-cost prokaryotic production methods. Despite these advantages, therapeutic development of antibody fragments remains challenging because the lack of an Fc domain results in loss of immune signaling, poor pharmacokinetics, and reduced bioavailability. Here, we use rational protein engineering approaches, supported by computational and experimental validation, to restore Fc receptor-mediated function and improve pharmacokinetics. Our long-term goal is to expand the relevance and accessibility of antibody fragments as therapeutics through lower-cost production and delivery.
Bio: I am in the final year of my PhD in Bioengineering in the lab of Professor Shannon Sirk. I received my bachelor’s degree in chemical engineering from Michigan State University, then spent two years as a research scientist in animal health biopharma before pursuing my PhD at the University of Illinois. My current work focuses on improving the accessibility of antibody-based therapeutics by engineering small antibody fragments to enhance therapeutic utility, improve pharmacokinetics, and enable alternative delivery strategies.