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Molecular basis of pathogenesis: Structure based design of novel therapeutics for the treatment of infectious diseases

  • Full or part time
  • Application Deadline
    Applications accepted all year round
  • Self-Funded PhD Students Only
    Self-Funded PhD Students Only

About This PhD Project

Project Description

Through the study of protein structure, primarily using protein crystallography but also electron microscopy and small-angle X-ray scattering, we aim to probe crucial biomolecular interactions central to a variety of diseases. The aim is to use this information to accelerate the development of new drugs and therapeutics.

Studies within the group focus on a variety of proteins from human and animal specific pathogens including bacterial adhesin molecules and potential drug target from trypanosomes. We also have an interest in both the design of novel proteins and artificial genomic systems. We employ a wide range of techniques from recombinant DNA technology, protein purification and characterisation, proteomics approaches through to structure determination using crystallography and molecular modelling. We adopt an interdisciplinary approach to the discovery of new therapeutics, frequently requiring working close to the industrial and academic medical biochemistry interface.

Webpage Link:


Antony J. Burton, Andrew R. Thomson, William M. Dawson, R. Leo Brady & Derek N. Woolfson (2016) ‘Installing hydrolytic activity into a completely de novo protein framework‘ Nature Chemistry DOI:10.1038/nchem.2555

Thomson, A. R., Wood, C. W., Burton, A. J., Bartlett, G. J., Sessions, R. B., Brady, R. L. & Woolfson, D. N. (2014) ‘Computational design of water-soluble α-helical barrels’ Science 346 (6208), 485-488

Zaccai NR, Chi B, Thomson AR, Boyle AL, Bartlett GJ, Bruning M, Linden N, Sessions RB, Booth PJ, Brady RL & Woolfson DN (2011) A de novopeptide hexamer with a mutable channel. Nature Chem Biol 7, 935-941

Agnew C, Borodina E, Zaccai NR, Conners R, Burton NM, Vicary JA, Cole DK, Antognozzi M, Virji M, & Brady RL (2011) Correlation of in situ mechanosensitive responses of the Moraxella catarrhalis adhesin UspA1 with fibronectin and receptor CEACAM1 binding. PNAS 108 (37), 15174-15178

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