Protein hydrogels have favorable utility compared to synthetic hydrogels in biomedical applications due to their inherent biodegradability, bioavailability, and biocompatibility. Among the thermoresponsive protein hydrogels, lower critical solution temperature (LCST) gels, which gel above a certain temperature, have been extensively characterized for their structural and mechanical properties, as well as their applicability in therapeutics delivery. Herein, we present a hydrogel that exhibits upper critical solution temperature (UCST) phase behavior, gelling below a critical temperature. The hydrogel described is based on a single coiled-coil protein, Q, which is an engineered variant of the coiled-coil domain of cartilage oligomeric matrix protein (COMPcc). Using transmission electron microscopy, Q has been shown to assemble into nanofibers, which then physically cross-link at low temperature, forming a hydrogel. Upon binding with the small hydrophobic molecule, curcumin, the Q hydrogel exhibits enhanced mechanical properties and thermostability in addition to a sustained release profile over time, demonstrating its potential in drug delivery applications.

Thermoresponsive fiber-based protein hydrogels for small molecule release

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.