Portal latinoamericano de toxicología
Self-illuminating polymers with the ability to home in on toxic prions and render them harmless
4 July, 2012
Prion busting molecules. cordis.europa.eu. June 15, 2012.Newly developed self-illuminating polymers have been intentionally designed with the ability to home in on toxic prions and render them harmless, offering the potential to cure fatal nerve-destroying illnesses. This Swedish-Swiss study was supported in part by the LUPAS (‘Luminescent polymers for in vivo imaging of amyloid signatures’) project, which is backed with almost EUR 5 million under the Health Theme of the EU’s Seventh Framework Programme (FP7). The findings were presented in The Journal of Biological Chemistry.
The research conducted here is truly groundbreaking. Researchers from Linköping University in Sweden, in cooperation with colleagues from the University Hospital of Zurich in Switzerland, said 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. They tested these luminescent conjugated polymers, or LCPs, on tissue sections infected with prions. The results indicate that the number of prions, as well as their toxicity and infectibility, decreased drastically.
‘When we see this effect on prion infections, we believe the same approach could work on Alzheimer’s disease as well,’ says Peter Nilsson, a researcher in Bioorganic Chemistry funded by the European Research Council (ERC).
Prion disease is a group of progressive conditions that affect the brain and nervous system of humans and animals. Human prion diseases include sporadic Creutzfeldt-Jakob disease, Kuru, variant Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker syndrome, and fatal familial insomnia. Prion illnesses can be inherited, occur spontaneously or through infection, for example through infected meat – as was the case with mad cow disease.
‘Based on these results, we can now customise entirely new molecules with potentially even better effect,’ Dr Nilsson said.
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.
The EU-funded LUPAS project, meanwhile, sought to bridge the gap between diagnosis and treatment of Alzheimer disease and prion diseases. At the beginning of the project the LUPAS team believed that by developing novel agents and methods for diagnostic imaging of amyloid plaque it would be possible to improve quality of diagnosis and facilitate monitoring and understanding of the disease progression.
The project gathered partners from a wide range of areas ranging from experts within organic synthetic chemistry, synthetic nano chemistry, amyloid structure, prion disease, Alzheimer’s disease, magnetic resonance imaging, multi-photon physics and hyper spectral imaging. They formed the critical mass of competences needed to reach towards the project’s ambitious goals.
LUPAS coordinator Professor Per Hammarstrom said at the launch of the project: ‘The competence within the LUPAS consortium will undoubtedly bring forward novel tools for understanding the pathological hallmarks of Alzheimer’s disease and prionoses. Within the three-year timeframe of LUPAS we will develop these tools for use in disease models systems in vivo and on histolological ex vivo samples from humans. If successful it will take a few more years to apply this technology in the clinic.’
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‘When we see this effect on prion infections, we believe the same approach could work on Alzheimer’s disease as well,’ says Peter Nilsson, a researcher in Bioorganic Chemistry funded by the European Research Council (ERC).
Prion disease is a group of progressive conditions that affect the brain and nervous system of humans and animals. Human prion diseases include sporadic Creutzfeldt-Jakob disease, Kuru, variant Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker syndrome, and fatal familial insomnia. Prion illnesses can be inherited, occur spontaneously or through infection, for example through infected meat – as was the case with mad cow disease.
‘Based on these results, we can now customise entirely new molecules with potentially even better effect,’ Dr Nilsson said.
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.
The EU-funded LUPAS project, meanwhile, sought to bridge the gap between diagnosis and treatment of Alzheimer disease and prion diseases. At the beginning of the project the LUPAS team believed that by developing novel agents and methods for diagnostic imaging of amyloid plaque it would be possible to improve quality of diagnosis and facilitate monitoring and understanding of the disease progression.
The project gathered partners from a wide range of areas ranging from experts within organic synthetic chemistry, synthetic nano chemistry, amyloid structure, prion disease, Alzheimer’s disease, magnetic resonance imaging, multi-photon physics and hyper spectral imaging. They formed the critical mass of competences needed to reach towards the project’s ambitious goals.
LUPAS coordinator Professor Per Hammarstrom said at the launch of the project: ‘The competence within the LUPAS consortium will undoubtedly bring forward novel tools for understanding the pathological hallmarks of Alzheimer’s disease and prionoses. Within the three-year timeframe of LUPAS we will develop these tools for use in disease models systems in vivo and on histolological ex vivo samples from humans. If successful it will take a few more years to apply this technology in the clinic.’
For more information, please visit:
LUPAS:
http://www.lupas-amyloid.eu
The Journal of Biological Chemistry:
http://www.jbc.org/