Molecules ‘light up’ Alzheimer’s roots

Molecules ‘light up’ Alzheimer’s roots

3:51 PM, 15th July 2011
Molecules ‘light up’ Alzheimer’s roots
Amyloid fibrils like those magnified here 12,000 times are thought to be the cause of plaques in the brains of Alzheimer's disease patients. Rice University researchers have created a metallic molecule that becomes strongly photoluminescent when it attaches to fibrils.

· A breakthrough in sensing could make finding signs of Alzheimer’s disease nearly as simple as switching on a light.

· The technique reported in the Journal of the American Chemical Society should help researchers design better medications to treat the devastating disease.

HOUSTON, US: The lab of Rice, Bioengineer, Angel Martí is testing metallic molecules that naturally attach themselves to a collection of beta amyloid proteins called fibrils, which form plaques in the brains of Alzheimer’s sufferers. When the molecules, complexes of dipyridophenazine ruthenium, latch onto amyloid fibrils, their photoluminescence increases fiftyfold.

The large increase in fluorescence may be an alternative to molecules currently used to study amyloid fibrils, which researchers believe form when misfolded proteins begin to aggregate.

Nathan Cook, a former Houston high school teacher and now a Rice graduate student and lead author of the new paper, began studying beta amyloids when he joined Martí’s lab. Cook’s goal was to find a way to dissolve amyloid fibrils in Alzheimer’s patients.

But the Colorado native’s research led him down a different path when he realized the ruthenium complexes, the subject of much study in Martí’s group, had a distinctive ability to luminesce when combined in a solution with amyloid fibrils.

Such fibrils are simple to make in the lab, he said. Ruthenium-based molecules added to the amyloid monomers do not fluoresce, Cook said. But once the amyloids begin to aggregate into fibrils that resemble “Microscopic strands of spaghetti,” hydrophobic parts of the metal complex are naturally drawn to them. “The microenvironment around the aggregated peptide changes and flips the switch” that allows the metallic complexes to light up when excited by a spectroscope, he said.

Thioflavin T (ThT) dyes are the standard sensors for detecting amyloid fibrils and work much the same way, Martí said.

Cook also exploited the metallic’s long-lived fluorescence by “time gating” spectroscopic assays. “The exciting part of this experiment is that traditional probes primarily measure fluorescence in two dimensions: intensity and wavelength. We have demonstrated that we can add a third dimension - time - to enhance the resolution of a fluorescent assay,” he said.

Cook’s goal remains the same: to treat Alzheimer’s - and possibly such other diseases as Parkinson’s - through the technique. He sees a path forward that may combine the ruthenium complex’s ability to target fibrils and other molecules’ potential to dissolve them in the brain.

Co-authors of the paper are recent Rice graduate Veronica Torres and Disha Jain, a former postdoctoral researcher in Martí’s lab. The Welch Foundation supported the research.

(C) Rice University News

 

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