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Characterising surface properties of protein biopharmaceutical molecules


Project Description

Protein biologicals have great potential for the effective treatment of a wide range of diseases. However, aggregation and instability are inherent issues with all protein pharmaceuticals, which is a problem that can limit their utility and developability. Therefore, a better understanding of the molecular basis of protein aggregation, along with the development of formulations to improve protein stability and solubility, would have a major impact on the generation of new therapeutics. Protein aggregation and self-association, as any protein-protein interaction, is primarily mediated by the surface of the molecules. Therefore, understanding the surface properties of proteins (including biopharmaceuticals), and how protein surface interacts with the chemicals used in formulations, is the key for producing improved therapeutics.

The aim of this project is to develop new approaches for the characterisation and probing of protein surface properties using solution NMR spectroscopy, and correlate these with theoretical calculations using the 3D structure of these proteins.

This multidisciplinary project will be carried out under the supervision of Drs Alexander Golovanov and Jim Warwicker. The student will receive extensive training in modern high-resolution multi-dimensional NMR techniques, protein modelling and computational biology. The School of Chemistry has state-of-the-art research facilities, including recent investment in the NMR facility that is now equipped with multichannel 500, 600 and 800 MHz spectrometers with cyroprobes. The supervisory team has strong links with industry, which will help to disseminate/ commercialise the discoveries made in this project to the biotechnology and biopharmaceutical sectors.

Contact for further Information:

Dr Alexander Golovanov

Funding Notes

Applications are invited from self-funded students. For UK/EU tuition fees are £15,500 and International are £30,500 for 2019/20 academic year.

Candidates are expected to hold (or be about to obtain) a minimum upper second class honours degree (or the overseas equivalent) in a related area / subject. Candidates with experience in molecular biology or with an interest in structural biology and NMR spectroscopy are encouraged to apply.

Please select PhD Biotechnology on the online application form.

References

Edwards JM, Derrick JP, van der Walle CF, Golovanov AP. 19F NMR as a Tool for Monitoring Individual Differentially Labeled Proteins in Complex Mixtures. Mol Pharm. 2018 Jul 2;15(7):2785-2796.

Kheddo P, Bramham JE, Dearman RJ, Uddin S, van der Walle CF, Golovanov AP. Investigating Liquid-Liquid Phase Separation of a Monoclonal Antibody Using Solution-State NMR Spectroscopy: Effect of Arg·Glu and Arg·HCl. Mol Pharm. 2017 Aug 7;14(8):2852-2860.

Austerberry JI, Dajani R, Panova S, Roberts D, Golovanov AP, Pluen A, van der Walle CF, Uddin S, Warwicker J, Derrick JP, Curtis R. The effect of charge mutations on the stability and aggregation of a human single chain Fv fragment. Eur J Pharm Biopharm. 2017 Jun;115:18-30.

Kheddo P, Cliff MJ, Uddin S, van der Walle CF, Golovanov AP. Characterizing monoclonal antibody formulations in arginine glutamate solutions using 1H NMR spectroscopy. MAbs. 2016 Oct;8(7):1245-1258.

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