Prions eliminated in mice brains
April 26, 2012
Researchers at Linköping University 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.
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.)
“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.
Researchers want to go even further 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.
Ref.: I. Margalith, et al., Polythiophenes inhibit prion propagation by stabilizing PrP aggregates, Journal of Biological Chemistry, 2012 [DOI: 10.1074/jbc.M112.355958 (open access)