Protein-based therapeutics are becoming a major fraction of the world’s approved drug portfolio and are now used to treat a variety of diseases such as diabetes and cancer. Although protein-based therapeutics have high efficacy, selectivity, and minimal side effects, they suffer from premature degradation <i>in vivo</i>, which increases cost of treatment and reduces patient compliance. As a result, numerous studies have been devoted to the development of polymeric carriers to provide controlled release of protein therapeutics. Our lab has developed a library of thermoresponsive polyesters (TR-PEs) inspired by poly(acrylamides) (PAs), polyoxazolines (POx), and thermoresponsive elastin-like peptides (ELPs). A modular synthetic design allows for polyesterification of a variety of N-substituted monomers, yielding a library of high molecular weight TR-PEs, which undergo a reversible hydrophilicity change at a lower critical solution temperature (LCST). The hydrophilic nature of TR-PEs prevents full dehydration above the LCST, resulting in the formation of viscous polymer-rich coacervates. The degradable polyester backbone facilitates quick hydrolytic degradation. These features make TR-PEs ideal carriers for the controlled release of therapeutically useful proteins, whose biological function is dependent on maintaining their native structure. In this work, the ability of these polymers to encapsulate a model protein, fluorescently-tagged bovine serum albumin (FITC-BSA), is illustrated. We present a robust delivery system that is able to efficiently encapsulate proteins without loss of activity and delivery them locally in a controlled manner.

Thermoresponsive, biodegradable polyesters: Tunable properties and efficient protein encapsulation

2019 Spring National Meeting

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