New ‘plaque destroying’ light therapy could prevent Alzheimer’s disease by blitzing dangerous proteins

Rogue brain proteins that trigger Alzheimer’s disease could be destroyed using cheap light therapy, according to new research.

An optic probe has been developed by scientists that glows over 100 times more brightly when it identifies the fine fibers, or fibrils, of amyloid beta that kill neurons.

The light then oxidizes the fibers to prevent them from clumping together in patients’ brains, which inhibits memory and makes them confused.

An estimated five-and-a-half million people in the United States suffer from Alzheimer’s, according to the Alzheimer’s Association.

Experts say this technique could be an inexpensive way for doctors to halt the disease before it impacts the brain’s memory and cognitive function.

Professor Angel Marti, an associate professor of chemistry at Rice University in the Houston, Texas, and his team developed the probe because light ‘is a cheap resource.’

He said light activation allows his team to have ‘exquisite control’ of oxidation.

Professor Marti said: ‘We imagine it might be possible someday to prevent symptoms of Alzheimer’s by targeting amyloid beta in the same way we treat cholesterol in people now to prevent cardiovascular disease.’

The clumping together of the amyloid beta is one of the main causes of dementia and Alzheimer’s, but drugs that target it have so far failed.

Build-up of the protein is one of the earliest changes seen in patients’ brains, forming sticky plaques and leading to nerve cell death and memory loss.

The probe pinpoints a specific binding site on the protein that could facilitate better drugs to treat the disease.

The device, described in the journal Chem, targets the fibrils using a rare metal called rhenium – and glows when hit with ultraviolet light.

But when it binds to the toxic protein it becomes more than 100 times brighter – causing it to oxidize.

‘While we cannot see the rhenium complex we can find the oxidation, or footprint, it produces on the amyloid peptide,’ Professor Marti said.

‘That oxidation only happens right next to the place where it binds. The real importance of this research is that it allows us to see with a high degree of certainty where molecules can interact with amyloid beta fibrils.’

Alzheimer’s is a degenerative brain disease that affects more than five million people living in the United States.

The symptoms can progress slow or gradual depending on the type of disease.

As the brain cells die in the brain, it causes memory loss and disorientation.

Previous research has studied the use of medication to target the fibrils in the brain that clump because of the disease.

But these medications have had difficulty targeting areas where the clumps occur.

Professor Marti said this device could help solve that problem.

‘There’s an interest in finding medications that will quench the deleterious effects of amyloid beta aggregates,’ Professor Marti said.

‘But to create drugs for these, we first need to know how drugs or molecules in general can bind and interact with these fibrils, and this was not well known.

‘Now we have a better idea of what the molecule needs to interact with these fibrils.’

He said the findings are important for the design of new drugs targeting amyloid beta.

If the resulting oxidation keeps the fibrils from aggregating further into the sticky substance found in the brains of Alzheimer’s patients, it offers hope of an effective treatment.

‘If we can modify complexes so they absorb red light, which is transparent to tissue, we might be able to perform these photochemical modifications in living animals, and maybe someday in humans,’ Professor Marti said.


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