Good news in the battle for the brain: Researchers in Sweden and
Switzerland have found that toxic prions diseased variants of naturally
occurring neural proteins can be both detected and treated with a novel
kind of self-illuminating polymer. In tests, the researchers have shown
that their molecules can render prions harmless, paving the way for
treatments for degenerative and potentially fatal nervous system
diseases, including Alzheimer’s.
Prions are a big problem when they get loose in the brain. They tend
to clump together in groups, affecting surrounding nerve cells and
usually leading to brain damage and eventually death—sometimes a very
rapid death. Illnesses caused by prions can be inherited, but they can
also be spontaneous or spread through infection, as is the case with mad
cow disease, a fairly well-known prion condition. Once prions begin
aggregating and replicating in the nervous tissue they can populate at
an exponential rate, making treatment very difficult.
The luminescent conjugated polymers, or LCPs, were tested at
University Hospital in Zurich on brain tissue taken from mice infected
with prions. Results from those tests showed that the number of prions
present in the tissue decreased significantly after the introduction of
LCPs, as did their overall toxicity—the first time such an effective
treatment has been demonstrated. LCPs still need a rigorous scientific
vetting of course, but the initial results are quite promising for the
future treatment of diseases like mad cow and Creutzfeldt-Jacobs.
Moreover, the results could have implications for the treatment of
that holy grail of neurological disorders, Alzheimer’s disease.
Alzheimer’s isn’t a prion disorder, strictly speaking. It is caused by
amyloid plaque buildup, which has a similar degrading effect on the
brain but one that is slower to take effect than those associated with
prion diseases. The researchers want to take their LCPs further and test
them on fruit flies imbued with an Alzheimer’s analog disorder to see
if they are effective at treating ailments similar to prion diseases as
well.
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