Dr John Viles
Reader in Biochemistry
Email: email@example.comTelephone: +44 (0)20 7882 8443Room Number: Room G.10, Joseph Priestley building
Protein misfolding in neurodegenerative diseases
Dr John Viles has an active research program studying protein misfolding associated with amyloid formation in neurodegenerative diseases. His team uses a range of biophysical techniques to study the fundamental process that influence neurotoxic oligomer and amyloid plaque formation. Approaches include, bimolecular spectroscopies, including NMR, CD, IR and EPR to study protein structure, misfolding and stability. In addition, florescent dyes, transmission electron microcopy and antibody binding are used to study the factors that influence the kinetics of fibre and oligomer formation.
The main research areas include:
- Copper and zinc in Alzheimer’s disease
- The structure and misfolding of the prion protein in TSE’s ‘mad-cow’ disease
- Amyloid-beta of Alzheimer’s disease and its protein binding partners.
Dr Viles received his Ph.D. from the University of London in 1994 and continued his research with Prof P Sadler (FRS) and Dame Prof J Thornton (CBE, FRS) studying metallo-proteins using NMR. In 1997 he took up a post-doctoral position with Prof P Wright at the Scripps Research Institute, California. In collaboration with the Nobel Laureate, Prof S Prusiner, he has published a number of significant papers on structure and function of the prion protein. Prions are the novel infectious agent of BSE and CJD in humans. He returned to the UK in 2000 to take up a lectureship position at Queen Mary and is currently a reader in biochemistry at Queen Mary, University of London.
- Find out more on Dr Viles' research website