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Effect of ELP Sequence and Fusion Protein Design on Concentrated Solution Self-Assembly
- Qin, Guokui, Perez, Paola M., Mills, Carolyn E., Olsen, Bradley D.
- Biomacromolecules 2016 v.17 no.3 pp. 928-934
- composite polymers, fluorescent proteins, hydrophobicity, latitude, models, molecular weight, nanomaterials, polypeptides, temperature
- Fusion proteins provide a facile route for the purification and self-assembly of biofunctional protein block copolymers into complex nanostructures; however, the use of biochemical synthesis techniques introduces unexplored variables into the design of the structures. Using model fusion constructs of the red fluorescent protein mCherry and the coil-like protein elastin-like polypeptide (ELP), it is shown that the molar mass and hydrophobicity of the ELP sequence have a large effect on the propensity of a fusion to form well-ordered nanostructures, even when the ELP is in the low temperature, highly solvated state. In contrast, the presence of a 6xHis purification tag has little effect on self-assembly, and the order of blocks in the construct (N-terminal vs C-terminal) only has a significant effect on the nanostructure when the conjugates are heated above the transition temperature of the ELP block. These results indicate that for a sufficiently hydrophobic and high molar mass ELP block, there is a great deal of design latitude in the construction of fusion protein block copolymers for self-assembling nanomaterials.