Project Description


Protein-based materials are currently leading to promising applications in various fields. With the advent of biotechnology, diverse assembly approaches have been developed to further acquire biomaterials with desired functionalities. Self-assembled protein Ultrabithorax (Ubx) from Drosophila melanogaster has been investigated as building blocks to construct material attributing to its inherent biocompatibility and mechanical properties. However, current yielding of Ubx has not achieved satisfactory results. The aim of our work was to develop a novel biomaterial by engineering the Ubx functional domain. We first identified Y167 and Y240 domains, dityrosine containing motifs contributing to the linkings forming self-assembly, and engineered them with mRFP afterwards to test its functions. It is concluded that Ubx has the potential to successfully incorporate diverse functional proteins for wide applications in various fields.


The versatility of biomaterial, along with its enhanced biocompatibility, biodegradability and lower immunogenicity has made its wide applications in various fields. In the past few years, different forms of fabricated protein have been developed to serve dynamic purposes, such as 3D printing bioink for tissue engineering, hydrogel for wound healing, scaffold for cell differentiation and beyond. Showing the enormous potential in a wide range of applications, biomaterial has further become our research topic. Eventually, we decided to seek out novelty in the field and develop a self-assembled biomaterial based on protein Ultrabithorax.

Why do we use Ultrabithorax protein?

Ultrabithorax (Ubx) is the Hox gene of Drosophila melanogaster. In addition to its well-known characteristic as a transcription factor, the unique in vitro features of Ubx have given it the advantages over many protein-based biomaterials.1

First, Ubx is biocompatible, biodegradable and non-immunogenetic. Those protein properties have highlighted their possible use in biomedicine. Second, Ubx possesses the ability to self-assemble into nanoscale fiber by forming crosslinking dityrosine bonds. Dityrosine containing motifs are the domains contributing to most self-assembly.2 Lastly, a study shows that Ubx can be readily functionalized with other proteins and retain its structure stability and mechanical properties afterwards.3

What have we achieved?

  1. We utilized binding region prediction model to identify dityrosine containing motifs Y167 and Y240 and engineered them with mRFP, and further proved the material has the potential to be incorporated with diverse functional proteins.
  2. We developed a protein-mixing model for scaffold simulation for further Ubx biomaterial implementation in tissue engineering and cell regeneratives.
  3. We utilized a 3D printer to bioprint our Ubx Biomaterial to achieve personalized design, high precision and on-demand creation of complex structure in a short period of time.
  4. We shared the knowledge of synthetic biology , promoted the concept of Ubx biomaterial, and built up efficient science communication by plans #BioArt_TheThirdSpace, #EdTech_GameSchooling and #SynBio_ Education Package & Ed Events.


  1. Pavlopoulos, A., & Akam, M. (2011, February 15). Hox gene ultrabithorax regulates distinct sets of target genes at successive stages of drosophila haltere morphogenesis. Proceedings of the National Academy of Sciences of the United States of America.
  2. Alexandra M. Greer, Zhao Huang, Ashley Oriakhi(2009, March 18). The Drosophila Transcription Factor Ultrabithorax Self-Assembles into Protein-Based Biomaterials with Multiple Morphologies Biomacromolecules 2009 10 (4),829-837
  3. Tsai, S.-P., Howell, D.W., Huang, Z., Hsiao, H.-C., Lu, Y., Matthews, K.S., Lou, J. and Bondos, S.E. (2015), The Effect of Protein Fusions on the Production and Mechanical Properties of Protein-Based Materials. Adv. Funct. Mater., 25: 1442-1450.