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Friday, April 27, 2012

Polythiophenes inhibit prion propagation


Polythiophenes inhibit prion propagation by stabilizing PrP aggregates

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Background: Luminescent conjugated polymers (LCPs) are highly specific to amyloid conformations and may represent potential antiprion compounds.

Results: LCPs significantly reduce prion titers, while rendering PrPSc more stable to proteolytic digestion.
Conclusion: LCPs possess pronounced antiprion potential and appear to act by compaction of frangible fibers.
Significance: LCPs may represent novel pharmacophores for the prevention and treatment of prion diseases.
“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.

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