Dr Simon Kolstoe
I gained a first class BSc in Biomedical Science at the University of Southampton before joining the laboratory of Professor Steve Wood for a PhD in Biochemistry. My doctoral project involved the use of X-ray crystallography in rational drug design for the pentraxin family of proteins.
In 2005 I took up a post-doctoral position working for Professor Sir Mark Pepys FRS at the Centre for Amyloidosis and Acute Phase Proteins, UCL Medical School. In 2006 our work on a depleter of C-reactive protein was published on the front cover of Nature. A second project, developing small molecules targeting the serum protein Transthyretin, contributed towards the group being awarded one of the first Wellcome Trust Seeding Drug Discovery Initiative awards in 2007. This latter work was subsequently patented and licensed to GSK in 2009. In 2010 I was promoted to Senior Post-doctoral Research Associate in the newly founded Wolfson Drug Discovery Unit where I continued working on similar projects this time in close collaboration with industrial partners and the NHS.
I joined the University of Portsmouth in April 2012 as a tenure-track Senior Fellow, and in 2014 received a BBSRC project grant to explore immune proteins, protein-DNA interactions and the use of mammalian cell lines for producing recombinant protein for biophysical characterisation.
Coupled to my biomedical research I have a bachelors degree in Philosophy and Master’s degree in Research Ethics. I am particularly interested in reporting bias and research ethics committee consistency. I chair the Hampshire A NHS research ethics committee, chair the MOD research ethics committee, am the University Ethics Advisor, and a member of the Department of Health's Confidentiality Advisory Group (CAG).
- Ethics committee review: quality and consistency
- Outcome reporting bias
- Expression of immune related proteins using the mammalian HEK293 system
- The function and structural biology of serum amyloid P component
- Structure based drug design (specifically relating to protein folding diseases)
- DNA-protein interactions