Study details how brain enzyme interacts with drug-like lead compound for Huntington's Disease
Researchers at the Manchester Institute of Biotechnology have detailed how an enzyme in the brain interacts with an exciting drug-like lead compound for Huntington's Disease to inhibit its activity. The research is published in the journal Nature.
Working with colleagues at the University of Leicester and the University of Lisbon in Portugal, the researchers identified the molecular structure of the enzyme kynurenine 3-monooxygense (KMO), which is found in the human brain. It took five years for the team to establish the crystal structure of KMO the first time it's ever been done.
The scientists then studied how the compound UPF 648 binds incredibly tightly to the enzyme to act as an inhibitor. Previous studies with animal models of neurodegenerative disease have showed that switching off the enzyme activity through drug binding should be effective in the treatment of brain disorders.
Professor Nigel Scrutton who led the study said: "UPF 648 works very well as an inhibitor of enzyme activity. However, in its current form it does not pass into the brain from the blood. The search is now on for related compounds that can both inhibit the enzyme and pass into the brain."
The findings from this research will now be used in the search for more effective treatments for Huntington's Disease.
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