Associate, Patent Attorney / London
Patents - biotechnology, chemistry & pharmaceuticals group
Matthew has a strong research background with technical expertise in molecular biology, biotechnology, biochemistry and organic chemistry.
Matthew's doctorate research at the University of Oxford investigated the mechanisms involved in the natural biosynthetic pathway of a clinically important antibiotic. Matthew subsequently undertook postdoctoral research at the University of British Columbia, where his work focused on the structures and mechanisms of enzymes linked to bacterial and viral pathogenesis. His research then took him to the MRC Laboratory of Molecular Biology in Cambridge, where he studied the immune response to HIV and influenza virus infections.
Matthew has published nine papers in peer-reviewed journals including Nature Structural & Molecular Biology, Angewandte Chemie and Nature Chemical Biology.
MChem in Chemistry, University of Oxford.
DPhil in Chemistry, University of Oxford (research part-funded by GlaxoSmithKline).
Certificate in Intellectual Property Law, Queen Mary, University of London.
Certificate in IP litigation.
Chartered Patent Attorney 2015.
European Patent Attorney 2015.
European Design Attorney.
Chartered Institute of Patent Attorneys (CIPA).
European Patent Institute (epi).
Caines, M.E. et al. Diverse HIV viruses are targeted by a conformationally dynamic antiviral. Nat. Struct. Mol. Biol. 19, 411-6 (2012).
Hancock, S.M. et al. Designer enzymes for glycosphingolipid synthesis by directed evolution. Nat. Chem. Biol. 5, 508-14 (2009).
Caines, M.E. et al. The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae, a potential target for structure-based vaccine design. J. Biol. Chem. 283, 31279-83 (2008).
Caines, M.E. et al. The structural basis of glycosidase inhibition by five-membered iminocyclitols. Angew. Chem., Int. Ed. 46, 4474-6 (2007).
Caines, M.E. et al. Structural and mechanistic analyses of endo-glycoceramidase II. J. Biol. Chem. 282, 14300-8 (2007).
Caines, M.E. et al. Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway. J. Biol. Chem. 279, 5685-92 (2004).