Guest lecture: Reengineering protein surfaces for non-aqueous activity

Prof. Adam Perriman, Bristol University, pioneer researcher in the construction and study of novel hybrid biomolecular systems using advanced physical techniques

25.08.2017 | Bianca Pérez

Dato fre 22 sep
Tid 10:15 11:00
Sted Aarhus University, building 1593, room 0.12

Biological macromolecules, such as proteins, have evolved to synergistically utilise the ensemble of forces that arise in an aqueous environment. Such forces help to drive protein folding and modulate dynamical behaviour, which in turn facilitates biological function. Although some enzymes can retain limited activity when extracted into anhydrous solvents, we have demonstrated that completely solvent-free (molten) functional protein liquids can be produced by remodelling the surface of a protein with a polymer surfactant. The electrostatically-grafted surfactant molecules act to extend the range of the intermolecular interactions, which allows the protein molecules to access an anhydrous liquid phase that is amenable to protein folding1, dynamics2 and function3.

These findings challenge the existing dogma that describes the role of water molecules in determining protein structure and function, and the robustness of this facile approach for achieving protein fluidity indicates that it could readily be developed for a wide range of biomolecules. Moreover, the development of the methodologies surrounding these novel hybrid constructs will not only provide insights into the role of water in protein folding, dynamics and function, but will also provide a gateway to the development of new technologies that will impact on industrial biocatalysis4 and regenerative medicine5.


1. Brogan, A. P. S., Siligardi, G., Hussain, R., *Perriman, A. W., Mann, S., Hyper-thermal stability and unprecedented re-folding of solvent-free liquid myoglobin. Chemical Science 2012, 3 (6), 1839-1846. DOI: 10.1039/c2sc20143g

2. Gallat, F.-X., Brogan, A. P. S., Fichou, Y., McGrath, N., Moulin, M., Haertlein, M., Combet, J., Wuttke, J., Mann, S., Zaccai, G., Jackson, C. J., *Perriman, A. W., *Weik, M., A Polymer Surfactant Corona Dynamically Replaces Water in Solvent-Free Protein Liquids and Ensures Macromolecular Flexibility and Activity. Journal of the American Chemical Society 2012, 134 (32), 13168-13171. DOI: 10.1021/ja303894g.

3. Perriman, A. W., Brogan, A. P. S., Coelfen, H., Tsoureas, N., Owen, G. R., *Mann, S., Reversible dioxygen binding in solvent-free liquid myoglobin. Nature Chemistry 2010, 2 (8), 622-626. DOI: 10.1038/NCHEM.700.

4. Brogan, A. P. S., Sharma, K. P., *Perriman, A. W., *Mann, S., Enzyme activity in liquid lipase melts as a step towards solvent-free biology at 150 degrees C. Nature Communications 2014, 5. DOI: 10.1038/ncomms6058.

5. Armstrong, J. P. K., Shakur, R., Horne, J. P., Dickinson, S. C., Armstrong, C. T., Lau, K., Kadiwala, J., Lowe, R., Seddon, A., Mann, S., Anderson, J. L. R., *Perriman, A. W., *Hollander, A. P., Artificial membrane binding proteins stimulate oxygenation of stem cells during engineering of large cartilage tissue. Nature Communications 2015, 6, 7405. DOI: 10.1038/ncomms8405

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