[Skip to content]

European Parkinson's Disease Association
Search our Site
.

Curcumin Prevents Aggregation in α-Synuclein by Increasing Reconfiguration Rate

Curcumin Prevents Aggregation in α-Synuclein by Increasing Reconfiguration Rate
xxx
Journal of Biological Chemistry Volume 287 Issue 12

16 March 2012
Ahmad B, Lapidus LJ


α-Synuclein is a protein that is intrinsically disordered in vitro and prone to aggregation, particularly at high temperatures.

In this work, we examined the ability of curcumin, a compound found in turmeric, to prevent aggregation of the protein. We found strong binding of curcumin to α-synuclein in the hydrophobic non-amyloid-β component region and complete inhibition of oligomers or fibrils. We also found that the reconfiguration rate within the unfolded protein was significantly increased at high temperatures.

We conclude that α-synuclein is prone to aggregation because its reconfiguration rate is slow enough to expose hydrophobic residues on the same time scale that bimolecular association occurs. Curcumin rescues the protein from aggregation by increasing the reconfiguration rate into a faster regime.