A Pinch of Saffron against Parkinson

This study from the University of Michigan, adds to the virtues of saffron and its compound, curcumin. This compound, or rather its mode of action could help prevent the clumping of proteins involved in the development of Parkinson's disease. These findings, published in the edition of the Journal of Biological Chemistry, identify a promising process that could inspire new therapeutic modes of action.

Turmeric or turmeric is a rhizome of a herbaceous plant of the same family as ginger. One of its extracts, Curcumin, extracted from turmeric, already known as a potent antioxidant protection against free radicals.

Lisa Lapidus, a physics professor and researcher at the University of Michigan and Basir Ahmad, a postdoctoral researcher had already demonstrated the involvement of alpha-synuclein proteins that aggregate in the early stages of Parkinson's disease. Their new study shows that curcumin blocks the aggregation of these proteins found in many neurological diseases. Curcumin binds strongly to alpha-synuclein aggregation and blocks.

The team used lasers to study protein folding. Proteins are chains of amino acids that perform most of the "work" in the cells. Scientists still know evil their construction process, linked to the speed at which the protein folds and its tendencies to aggregate. When curcumin binds to the protein alpha-synuclein not only does it stop the aggregation process but also increases the rate of folding and reconfiguration of the protein. This is increasing the speed of reconfiguration that curcumin prevents proteins from clumping.

The process identified from curcumin, attachment of the protein alpha-synuclein, could help scientists develop new drugs operating on the same principle. This is not curcumin itself whose active ingredient is difficult to replicate in the brain, but the process of blocking the proteins involved, prior to aggregation, which opens today new therapeutic approaches.

Source: Journal of Biological Chemistry
“Curcumin Prevents Aggregation in α-Synuclein by Increasing Reconfiguration Rate”

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