March 21, 2012. Research conducted at Michigan State University discovered that curcumin, a compound found in turmeric, helps prevent clumping of alpha-synuclein, a protein whose aggregation is one of the first steps in Parkinson's disease. The study was described in an article published in the March 16, 2012 issue of the Journal of Biological Chemistry. In earlier research, Michigan State associate professor of physics and astronomy Lisa Lapidus and postdoctoral researcher Basir Ahmad demonstrated that a decrease in the speed of folding or reconfiguration of alpha-synuclein increases its tendency to clump with other proteins. In the current study, the duo showed that attachment of curcumin to alpha-synuclein stops clumping and increases its folding rate, moving it out of the zone at which it is likely to clump. "We conclude that alpha-synuclein is prone to aggregation because its reconfiguration rate is slow enough to expose hydrophobic residues on the same timescale that bimolecular association occurs," the authors write. "Curcumin rescues the protein from aggregation by increasing the reconfiguration rate into a faster regime."
"Our research shows that curcumin can rescue proteins from aggregation, the first steps of many debilitating diseases," Dr Lapidus stated. "More specifically, curcumin binds strongly to alpha-synuclein and prevents aggregation at body temperatures."
"Curcumin's usefulness as an actual drug may be pretty limited since it doesn't go into the brain easily where this misfolding is taking place," she added. "But this kind of study showcases the technique of measuring reconfiguration and opens the door for developing drug treatments."
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