Thermoresponsive Protein-Engineered Coiled-Coil Hydrogel for Sustained Small Molecule Release
| Autor: | P. Douglas Renfrew, Lindsay K. Hill, Richard Bonneau, Jin Kim Montclare, Sean C O'Neill, Che Fu Liu, Michael Meleties, Xuan Xie, Raymond S. Tu, Priya Katyal, Erika Delgado-Fukushima, Youssef Zaim Wadghiri, Teeba Jihad |
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| Rok vydání: | 2019 |
| Předmět: |
Polymers and Plastics
Polymers Protein domain Bioengineering 02 engineering and technology 010402 general chemistry Protein Engineering 01 natural sciences Biomaterials Protein Domains Upper critical solution temperature Materials Chemistry Thermostability Coiled coil Drug Carriers Chemistry technology industry and agriculture Temperature Proteins Hydrogels Protein engineering 021001 nanoscience & nanotechnology Small molecule 0104 chemical sciences Nanofiber Delayed-Action Preparations Self-healing hydrogels Biophysics 0210 nano-technology Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Biomacromolecules. 20(9) |
| ISSN: | 1526-4602 |
| Popis: | Thermoresponsive hydrogels are used for an array of biomedical applications. Lower critical solution temperature-type hydrogels have been observed in nature and extensively studied in comparison to upper critical solution temperature (UCST)-type hydrogels. Of the limited protein-based UCST-type hydrogels reported, none have been composed of a single coiled-coil domain. Here, we describe a biosynthesized homopentameric coiled-coil protein capable of demonstrating a UCST. Microscopy and structural analysis reveal that the hydrogel is stabilized by molecular entanglement of protein nanofibers, creating a porous matrix capable of binding the small hydrophobic molecule, curcumin. Curcumin binding increases the α-helical structure, fiber entanglement, mechanical integrity, and thermostability, resulting in sustained drug release at physiological temperature. This work provides the first example of a thermoresponsive hydrogel comprised of a single coiled-coil protein domain that can be used as a vehicle for sustained release and, by demonstrating UCST-type behavior, shows promise in forging a relationship between coiled-coil protein-phase behavior and that of synthetic polymer systems. |
| Databáze: | OpenAIRE |
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