Neuroscience

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Rice opens new window on Parkinson’s disease
Rice University scientists have discovered a new way to look inside living cells and see the insoluble fibrillar deposits associated with Parkinson’s disease.
The combined talents of two Rice laboratories – one that studies the misfolded proteins that cause neurodegenerative diseases and another that specializes in photoluminescent probes – led to the spectroscopic technique that could become a valuable tool for scientists and pharmaceutical companies.
The research by the Rice labs of Angel Martí and Laura Segatori appeared online today in the Journal of the American Chemical Society.
The researchers designed a molecular probe based on the metallic element ruthenium. Testing inside live neuroglioma cells, they found the probe binds with the misfolded alpha-synuclein proteins that clump together and form fibrils and disrupt the cell’s functions. The ruthenium complex lit up when triggered by a laser – but only when attached to the fibril, which allowed aggregation to be tracked using photoluminescence spectroscopy.

Rice opens new window on Parkinson’s disease

Rice University scientists have discovered a new way to look inside living cells and see the insoluble fibrillar deposits associated with Parkinson’s disease.

The combined talents of two Rice laboratories – one that studies the misfolded proteins that cause neurodegenerative diseases and another that specializes in photoluminescent probes – led to the spectroscopic technique that could become a valuable tool for scientists and pharmaceutical companies.

The research by the Rice labs of Angel Martí and Laura Segatori appeared online today in the Journal of the American Chemical Society.

The researchers designed a molecular probe based on the metallic element ruthenium. Testing inside live neuroglioma cells, they found the probe binds with the misfolded alpha-synuclein proteins that clump together and form fibrils and disrupt the cell’s functions. The ruthenium complex lit up when triggered by a laser – but only when attached to the fibril, which allowed aggregation to be tracked using photoluminescence spectroscopy.

Filed under brain parkinson's disease alpha-synuclein proteins photoluminescence spectroscopy neuroscience science

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