Drug targets and validation

Drug validation is the process whereby the role of a potential drug target (eg a membrane receptor) in a disease is clearly defined and so can become a target for drug development. The theme of Drug Targets and Validation at Bristol exists to achieve the above and to facilitate mutually beneficial research interactions with the drug industry.

Focussed mainly within the School of Physiology and Pharmacology, members of this theme are interested in:

  • Developing chemical tools and technologies to facilitate biomedical research;
  • Defining cell processes as valid targets for drug intervention;
  • Developing drugs with potential therapeutic applications.

Our research areas

  • Developing chemical tools and technologies to facilitate biomedical research
  • Defining cell processes as valid targets for drug intervention
  • Developing drugs with potential therapeutic applications
  • Excitatory amino acids
  • Learning and memory
  • Neural-vascular interactions
  • Cardiac arrhythmias
  • Neuronal control of respiration
  • Cystic Fibrosis
  • Heart disease and arrhythmias
  • Neurogenic hypertension
  • Opioids, pain and drug abuse
  • Neuropathic pain
  • Platelet signalling and drug action
  • Depression and schizophrenia
  • Wound healing
  • Arthritis
  • Neural mechanisms of obesity
  • Dementia
  • Cerebellar dysfunction

Research technologies in use

  • Models of disease; depression, anxiety, pain, dementia, heart failure, arrhythmias, Down’s Syndrome, Rett syndrome  and hypertension
  • Molecular modelling
  • Organic synthesis and medicinal chemistry
  • Advanced imaging (TIRF, electron microscopy)
  • Brain slice electrophysiology
  • Single-channel patch-clamp recording
  • Cell signalling assays
  • Primary neuronal culture
  • Zebrafish and drosophila models
  • Proteomics

Ongoing collaborations with industry

Collaboration opportunities and contacts

To find out more, explore our research pages. To discuss possibilities for collaboration or to find out more, please contact us.

Email phph-adminsupport@bristol.ac.uk

High affinity GluK1 antagonist UBP310 in the X-ray crystal structure of the ligand binding domain of GluK1
High affinity GluK1 antagonist UBP310 in the X-ray crystal structure of the ligand binding domain of GluK1.
Edit this page