A breakthrough for neurodegenerative disease researchers in an attempt to find a treatment for Parkinson's disease and Huntington's disease
A breakthrough for neurodegenerative disease researchers in an attempt to find a treatment for Parkinson's disease and Huntington's disease. Researchers have identified an enzyme in the brain that inhibits the activity of a leading Huntington's disease drug-like substance. The group of researchers claims that the findings show that the substance can be developed as an effective treatment against neurodegenerative diseases. It took 5 years for the group of researchers to create a crystal structure of the enzyme for the first time ever
By James Rush Published in MAIL ONLINE
On April 10, 2013.
A significant breakthrough has been achieved by researchers looking for a treatment for neurodegenerative diseases such as Parkinson's disease. Researchers at the Manchester Institute of Biotechnology have detailed how an enzyme in the brain reacts with a substance similar to a leading Huntington's disease drug to inhibit its activity. The group of researchers claims that its findings show that it can be developed as an effective treatment for neurodegenerative diseases such as Huntington's disease, Alzheimer's and Parkinson's. Collaboration with researchers at the University of Leicester and the University of Lisbon in Portugal led to the identification of the molecular structure of the kynurenine 3-monooxygenase (KMO) enzyme in the human brain. It took 5 years for the team of researchers to determine the crystal structure of KMO, the first time this was done. The researchers, who published their work in NATURE, went on to study how a substance called UPF 648 binds tightly to the enzyme and works to inhibit its activity. Previous studies in animal models in models for neurodegenerative diseases that turning off the activity of the enzyme by binding a drug should be effective in the treatment of brain diseases. Research director Professor Nigel Scruton said: "UPF 648 works well as an enzyme activity inhibitor. But in its current form it does not enter the brain from the blood. Research is now focused on finding similar substances that will both act against the enzyme and enter the brain from the blood." He added: "Our research that detailed the molecular structure of the enzyme allows us to look for new KMOs that are able to cross the blood-brain barrier. This gives real hope for the development of drug treatments against neurodegenerative diseases such as Huntington's, Alzheimer's and Parkinson's disease."
Dr. Flaviano Giorgini, the group's neurogeneticist from the University of Leicester, said: "This is a big step forward on the way to developing KMO-inhibiting drugs. We hope that such substances will be tested in clinical trials and prove to be effective for patients."
The research findings will be used from now on to search for more effective treatments for Huntington's disease.
Professor Sarah Tabrizi, head of the Huntington's disease research group at University College London's Institute of Neurology said: "Deciphering the crystal structure of KMO is a big step forward in advancing our efforts to find treatments for this deadly disease. It allows a solid basis for optimizing inhibitory drugs like UPF 648 that are being developed by a community The global study of Huntington's disease. KMO is one of our most prominent targets for drug development, and the crystal structure is a significant step along our road map to clinical trials of KMO inhibitors in patients."
Kat Stanley, chairwoman of the Huntington's Disease Association welcomes the results. She said: "This research is a really exciting piece of kit that slightly improves our understanding and brings us one step closer to being able to provide an effective treatment for Huntington's disease.
