Department of Biology & Biochemistry

david_brown

Professor of Biochemistry

4 South 1.46

Email: bssdrb@bath.ac.uk

Tel: +44 (0) 1225 383133 

 
 

Current Funding

  • Alzheimer's Research UK
  • BRACE

Coworkers

  • Dr. Jennifer McDowall
  • Hazel Roberts
 

Prof David Brown 

Profile

Our research focuses on proteins associated with neurodegenerative diseases including Alzheimer’s disease, Parkinson’s disease and the so called prion diseases. Prion diseases include the notorious Bovine Spongiform Encephalopathy and the human diseases vCJD, sporadic CJD and Fatal Familial Insomnia. However, despite the concern about these disease the prion protein is a harmless neuronal protein expressed in all vertebrates. Our group is concerned with the normal function of this protein. The prion protein is a copper binding protein which appears to be involved in cellular resistance to oxidative stress. Only when the protein is converted to an abnormal isoform is it capable of inducing neuronal death. Alpha-synuclein can also be converted to a toxic form by its interaction with copper. We are currently studying the mechanism of this process.

Protein Studies

Research from our group has been instrumental in showing that the prion protein is a copper binding protein. Our current research includes new directions to study other metal binding proteins associated with neurodegenerative diseases. We have been studying the synuclein family of proteins and the copper and iron binding abilities. We are further investigating the metal binding of these proteins using exciting techniques such isothermal titration calorimetry, EPR and cyclic voltammetry. In particular, the redox chemistry of these proteins on binding metals is important to determine, as all three diseases are associated with oxidative damage to the brain.

Cell Studies

We also use cell culture to investigate the function of proteins such as alpha-synuclein and APP. We have recently shown that alpha-synuclein is active in cells to reduce iron to Fe(II). We are investigating the further implications of this exciting breakthrough.

Professor Brown welcomes any enquires regarding Ph.D. opportunities. The group is also open to collaborations with other researchers or industrial partners. 

Publications

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