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Dr John Viles

John

Reader in Biochemistry and Director of Biochemistry Programme

Email: j.viles@qmul.ac.uk
Telephone: +44 (0)20 7882 8443
Room Number: Room G.10, Joseph Priestley building

Undergraduate Teaching

  • Practical Molecular and Cellular Biology (Tutorials) (BIO190)
  • Practical Biochemistry (Tutorials) (BIO198)
  • Biochemistry Communication (year 2) (BIO201)
  • Techniques for Biological and Chemical Sciences (BIO269)
  • Advanced Biochemical Research Methods (BIO491)
  • Techniques in Biomedical Sciences (BMD219)
  • Biochemistry Communication (BIO301)
  • Protein Structure, Folding and Assemblies (BIO367)
  • Molecular Basis of Disease (BIO363)

Research

Research Interests:

Find out more on Dr Viles' research website

Protein misfolding in neurodegenerative diseases

John Viles has an active research program studying protein misfolding associated with amyloid formation in neurodegenerative diseases. His team uses a range of biochemical/biophysical techniques to study the fundamental process that influence neurotoxic oligomer and amyloid plaque formation in Alzheimer’s, Parkinson’s and Prion (Mad Cow) disease.  Approaches include, bimolecular spectroscopies (including NMR, CD) and microscopy at the molecular resolution (cryo-Transmission Electron and Atomic Force Microscopy) to study protein misfolding and amyloid assembly.

Dr John H. 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 and director of taught programs in Biochemistry. 

Main research areas include:

1. Amyloid – lipid membrane interactions and ion channel formation

Amyloid – lipid membrane interactions and ion channel formation featured in Chemical Science

 

 

 

 

 

 

 

 

phospholipid bilayer phospholipid bilayer

 

 

 

 

Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy DC Bode, M Freeley, J Nield, M Palma, JH Viles* (2019) J of Biol Chem (accelerated communication)

Ion Channel Formation by Amyloid-β42 Oligomers but not Amyloid-β40 in Cellular Membranes DC Bode, MD Baker*, JH Viles* (2017) J of Biol Chem

2. Copper and Zinc in Alzheimer’s disease

line graph showing Truncated Amyloid binding to copper

 

 

 

 

Truncated Amyloid-β (11-40/42) from Alzheimer's Disease Binds Copper2+ with a Femtomolar Affinity and Influences Fibre Assembly
J D Barritt, J H. Viles*(2015) J of Biol Chem,

The Rapid Exchange of Zinc2+ Enables Trace Levels to Profoundly Influence Amyloid-β Misfolding and Dominates Assembly Outcomes in Cu2+/Zn2+ Mixtures
C J Matheou, N D Younan, J H Viles* (2016) J Mol Biol

Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, Zinc and Iron in Alzheimer's, Parkinson's and Prion disease
JH Viles* (2012) Coordination Chemistry Reviews 

3. Co-Fibrilization of amyloid proteins

Amyloid proteins

 

N‐Terminally Truncated Amyloid‐β (11‐40/42) Co‐Fibrillises with its Full‐Length Counterpart. Implications for Alzheimer's Disease JD Barritt, ND Younan, JH Viles* (2017) Angewandte Chemie

 

 

4. Amyloid-beta of Alzheimer’s disease and its protein binding partners

Graph showing Amyloid fibre over time

Serum Albumin’s Protective Inhibition of Amyloid-β Fibre Formation is Suppressed by Cholesterol, Fatty Acids and Warfarin
DC. Bode, HF. Stanyon, T Hirani, MD. Baker, J Nield, JH. Viles*
(2018) J Mol Biol 

 

5. The structure and misfolding of the prion protein in TSE’s ‘mad-cow’ disease

Prion protein stabilizes amyloid-β oligomers and enhances their neurotoxicity in a Drosophila model of Alzheimer's disease

Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in a Drosophila model of Alzheimer's disease
ND Younan, KF Chen, RS Rose,
DC Crowther, JH Viles
(2018) J of Biol Chem

 

 

 

 

Copper(II) binding to the prion protein. Structural implications JH Viles$ Fred E Cohen, Stanley B. Prusiner, Peter E Wright* and H Jane Dyson* (1999) Proc Natl Acad Sci

Structure of the Recombinant Full-Length Hamster Prion Protein PrP(29-231)
DG Donne$, JH Viles$, Stanley B. Prusiner, Peter E. Wright*, and H. Jane Dyson*
(1997) Proc Natl Acad Sci ($ joint first author)

Research department

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