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Curcumin Reduces Amyloid Beta Oligomer Interactions with Anionic Membranes.
Chad A Sallaberry1, Barbie J Voss1, William B Stone1
1Department of Chemistry and Biochemistry, University of Colorado Colorado Springs, Colorado Springs, Colorado 80918, United States.
ACS Chemical Neuroscience
|October 31, 2023
Summary
Curcumin inhibits amyloid-beta fibrillar oligomer (FO) aggregation on anionic membranes by altering membrane structure and interacting with FO. This dual action reduces FO accumulation, offering insights into Alzheimer
Area of Science:
- Biochemistry
- Neuroscience
- Materials Science
Background:
- Neurodegenerative diseases like Alzheimer's involve amyloidogenic proteins, such as amyloid-beta (Aβ), forming aggregates on cell membranes.
- Curcumin, a polyphenol, interacts with membranes and affects Aβ aggregation, making it a key molecule for studying these processes.
Purpose of the Study:
- To investigate the interactions between curcumin, Aβ fibrillar oligomers (FO), and anionic membranes.
- To elucidate the molecular mechanisms by which curcumin modulates Aβ aggregation at membrane surfaces.
Main Methods:
- Utilized liquid surface X-ray scattering experiments to study membrane structure and protein-lipid interactions.
- Employed molecular dynamics simulations to visualize curcumin-membrane and curcumin-Aβ interactions at the atomic level.
Main Results:
- Curcumin embeds into anionic 1,2-dimyristoyl-sn-glycero-3-phosphorylglycerol (DMPG) membranes, causing disorder and thinning.
- Curcumin reduced FO accumulation on DMPG membranes by approximately 66%, attributed to membrane thinning and direct interactions.
- Simulations showed curcumin clustering near phenylalanine residues on membrane-bound FO.
Conclusions:
- Curcumin inhibits FO interaction with anionic membranes through a combination of altering membrane properties and direct binding to the FO surface.
- This study clarifies curcumin's mechanism in inhibiting amyloidogenesis via dual membrane and protein interactions.
