Protein-based hydrogels are known for their biocompatibility and biodegradability, as well as their high water content and tunable viscoelasticity, which allow them to be used as injectable biomaterials. The N-terminus of the Cartilage Oligomeric Matrix Protein, COMPcc, is a pentameric coiled-coil motif with an axial hydrophobic pore for binding a variety of small molecules such as doxorubicin, vitamin A, vitamin D, and curcumin. Our group has engineered a mutant of this domain dubbed Q, which maintains patches of positive and negative surface charges, allowing the protein to self-assemble into nanofibers. After native purification of Q at pH 8, it assembles into a hydrogel with a concentration as low as 1mM at 4C within just 36 hours. ATR-FTIR studies confirm that the coiled-coil secondary structure of the Q-hydrogel is comparable to that of chemically crosslinked Q mesofibers. These findings suggest that Q may serve as spontaneously forming hydrogels for applications including drug delivery and tissue engineering.<br/>

Hydrogel formation with self-assembly fibrous coiled-coil protein

254th National Meeting (2017)

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