T. Wright
University of California, Los Angeles,
United States
Keywords: enzyme, bioconjugation, polymer
Summary:
Protein-polymer conjugation has emerged as a promising strategy to enhance the stability, solubility, and activity of enzymes and therapeutic proteins for drug delivery applications. In this work, we explore how different polymer types, including cationic, anionic, and hydrogen-bonding polymers, can modify enzyme stability and activity. Specifically, we demonstrate the successful conjugation of enzymes with functional polymers, which results in significant enhancements in activity and resistance to denaturing conditions. Polymer chain length and the nature of polymer–protein interactions were shown to be critical in tuning enzymatic performance, particularly under extreme conditions such as high temperatures and organic solvents. Additionally, we introduce a novel method for site-specific conjugation using hydrolytically stable maleimide-functionalized polymers, which could be advantageous for controlled drug release. These insights open new possibilities for the design of stable, high-performance conjugates in drug delivery systems, enabling improved therapeutic outcomes in challenging environments.