Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 12, Pages 9193-9199Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.325548
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Funding
- National Science Foundation [MCB-0825001]
- Michigan State University High Performance Computing Center
- Institute for Cyber Enabled Research
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alpha-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 alpha-synuclein in the hydrophobic non-amyloid-beta 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 alpha-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.
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