This new study led by Ahmal shows that curcumin binds to alpha-synuclein and thus prevents it from aggregating in neurons. Lisa Lapidus, MSU associate professor of physics said: “Our research shows that curcumin can rescue proteins from aggregation, the first steps of many debilitating diseases. More specifically, curcumin binds strongly to alpha-synuclein and prevents aggregation at body temperatures.”
http://www.doctortipster.com/8831-cu...new-study.html
Curcumin prevents aggregation in α-synuclein by increasing the reconfiguration rate
Basir Ahmad and Lisa J. Lapidus*
+ Author Affiliations
Michigan State University, United States
↵* Corresponding author; email:
lapidus@msu.edu
Capsule
Background: α-synuclein is an aggregation-prone protein which reconfigures more slowly under aggregating conditions.
Results: Curcumin binds to monomeric α-synuclein, prevents aggregation and increases the reconfiguration rate, particularly at high temperatures.
Conclusion: Curcumin rescues the protein from aggregation by making the protein more diffusive.
Significance: The search for aggregation inhibitors should account for changes in chain dynamics by the small molecule.
Abstract
α-synuclein is a protein that is intrinsically disordered in vitro and prone to aggregation particularly at high temperatures. In this work we examine the ability of curcumin, a compound found in turmeric, to prevent aggregation of the protein. We find strong binding of curcumin to α-synuclein in the hydrophobic non-amyloid-β component (NAC) region and a complete inhibition of oligomers or fibrils. We also find that the reconfiguration rate within the unfolded protein is 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 timescale that bimolecular association occurs. Curcumin rescues the protein from aggregation by increasing the reconfiguration rate into a faster regime.
http://www.jbc.org/content/early/201...bc.M111.325548