Professor Paul A. Dalby
Department of Biochemical Engineering, University College London
What causes a therapeutic protein aggregate?
Can we predict good formulations to keep proteins stable for 2 years?
Are there more efficient ways to engineer novel activities and improved stability into enzymes?
Can directed evolution approaches be improved?
These are the questions we are trying to answer, and provide both experimental and computational solutions to. Several approaches are combined to answer these major challenges:
Research Activities:
Biophysical analyses to elucidate the causes of protein aggregation in therapeutic formulations, and in biocatalytic processes
Rational Protein Engineering and Directed Evolution to improve enzymes for Industrial Biotechnology
Develop high-throughput techniques to rapidly evaluate protein structure and function, such as biocatalytic conversions, protein formulations, freeze-drying, precipitation, and protein refolding.
Molecular dynamics simulations to evaluate protein stability and formulations in different environments.
Funding for the above research has come from the UK BBSRC, EPSRC, the TSB Technology Programme and a range of company collaborators.