The Molecules Used To Find Prions Found To Destroy Them As Well Possibly Leading To New Treatments For Brain Disease

 Mad Cow Disease

Toxic prions in the brain can be detected with self-illuminating polymers. The originators of the technique, at Linköping University in Sweden, have now shown that the same molecules can also render the prions harmless, and potentially cure fatal nerve-destroying illnesses such as mad cow disease and Alzheimer's.

Researchers at Linköping University in Sweden have found that luminescent conjugated polymers (LCPs) can render prions harmless and potentially cure fatal nerve-destroying illnesses, in addition to detecting the toxic molecules, as previously known.

The researchers and their colleagues at the University Hospital in Zürich tested the LCPs on tissue sections from the brains of mice that had been infected with prions.

The results show that the number of prions, as well as their toxicity and infectibility, decreased drastically. This is the first time anyone has been able to demonstrate the possibility of treating illnesses such as mad cow disease and Creutzfeldt-Jacobs with LCP molecules, the researchers say.

"When we see this effect on prion infections, we believe the same approach could work on Alzheimer's disease as well," says Peter Nilsson, researcher in Bioorganic Chemistry funded by ERC, the European Research Council.

Along with professors Per Hammarström and Adriano Aguzzi and others, he is now publishing the results in The Journal of Biological Chemistry.

Prions are diseased forms of normally occurring proteins in the brain. When they clump together in large aggregates, nerve cells in the surrounding area are affected, which leads to serious brain damage and a quick death. Prion illnesses can be inherited, occur spontaneously or through infection, for example through infected meat — is was the case with bovine spongiform encephalopathy (BSE), also known as “mad cow disease.” (The fourth case of  BSE in the U.S. was confirmed in a dairy cow in central California by the U.S. Department of Agriculture said on Tuesday April 24.)

The course of the illness is relentless when the prions fall to pieces and replicate at an exponential rate. When researchers inserted the LCP molecules into their model system, the replication was arrested, possible through stabilizing the prion aggregates.

“Based on these results, we can now customize entirely new molecules with potentially even better effect. These are now being tested on animal models,” Nilsson says.

The researchers now want to extend their exploration and test whether the molecules will function on fruit flies with an Alzheimer’s-like nerve disorder. Alzheimer’s is caused by what is known as amyloid plaque, which has a similar but slower course than prion diseases.


SOURCES  EurekAlert, Linkoping University

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