Designing modular protein scaffolds to study growth factors’ synergy: how splitting modular synthetic proteins into self-assembling parts affects overall expression and structure (360G-Wellcome-211723_Z_18_Z)

Growth factors control the fate of stem cells but it is still unclear how their organization and synergy contributes to cell proliferation and differentiation. To study these effects, molecules that can precisely display multiple growth factors need to be developed. Modular proteins, formed by repetitive units, can be designed to have very complex structures and their length can usually be changed easily. In this project I aim to express a modular protein, which has been computationally designed, in E. coli both as a whole protein and as self-assembling peptide blocks. I will use split inteins to allow multiple peptide fragments to join and bond to produce the desired modular protein. The aim of this research is to investigate how using self assembling blocks of peptides affects the yield of the final modular protein product when expressed in E. coli and to find whether or not expressing a modular protein in the form of self assembling blocks changes its structure compared to expressing the same protein as one polypeptide chain initially. These results will help understand how to better produce modular proteins to display growth factors and study effects of signal organization on cell response.