Constructing replacements for damaged or diseased organs or tissues requires scaffolds that support cell growth in 3-dimensions and factors that regulate cell behavior. The existing methods (physical trapping, chemical crosslinking, etc.) to generate biomaterials are often performed in harsh conditions and usually harm the sensitive molecules, such as proteins. Therefore, an effective and mild approach to generate the functional scaffold is needed.We have discovered that the Drosophila melanogasterprotein Ultrabithorax (Ubx) rapidly self-assembles into material in mild aqueous buffers at the air-liquid interface. Ubx material shows elastic and extensible properties and is able to hierarchically self-associate into structures ranging from nanoscale fibrils to macroscale fibers, films, and meshes.We then examined whether proteins with different physicochemical properties can successfully express, solubilize, fold and finally be assembled into material when fused to Ubx. To address it, we fused more than 20 proteins that have different sizes, charges, and structural conformations to Ubx. The results indicated that successful Ubx-fusions cover a broad range of physicochemical properties and show consistent ability to self-assemble into material.Furthermore, by circular dichroism (CD) spectroscopy, fluorescence spectroscopy and enzymatic experiments, we showed that proteins still retain their native structures and functions when fused to Ubx and assembled into materials. We also proved that Ubx materials with growth factor fusions not only provide cell attachment but also trigger signaling transduction in several cell types. In future, we aim to utilize the advantages of Ubx materials to control cell behaviors in 3-dimesional cell culture and tissue engineering.

Self-assembly and functionalization of Drosophila transcription factor Ultrabithorax

247th National Meeting (2014)

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