The Effects of Resveratrol, Caffeine, β-Carotene, and Epigallocatechin Gallate (EGCG) on Amyloid-  Aggregation in Synthetic Brain Membranes.
SCOPE
Alzheimer's disease is a neurodegenerative condition marked by the formation and aggregation of amyloid-β (Aβ) peptides. There exists, to this day, no cure or effective prevention for the disease; however, there is evidence that a healthy diet and certain food products can slow down first occurrence and progression. To investigate if food ingredients can interact with peptide aggregates, synthetic membranes that contained aggregates consisting of cross-β sheets of the membrane active fragment A  are prepared.


METHODS AND RESULTS
The impact of resveratrol, found in grapes, caffeine, the main active ingredient in coffee, β-carotene, found in orange fruits and vegetables, and epigallocatechin gallate (EGCG), a component of green tea, on the size and volume fraction of Aβ aggregates is studied using optical and fluorescence microscopy, X-ray diffraction, UV-vis spectroscopy, and molecular dynamics simulations. All compounds are membrane active and spontaneously partitioned in the synthetic brain membranes. While resveratrol and caffeine lead to membrane thickening and reduced membrane fluidity, β-carotene and EGCG preserve or increase fluidity.


CONCLUSION
Resveratrol and caffeine do not reduce the volume fraction of peptide aggregates while β-carotene significantly reduces plaque size. Interestingly, EGCG dissolves peptide aggregates and significantly decreases the corresponding cross-β and β-sheet signals.
['Gastaldo|Isabella P|IP|', 'Himbert|Sebastian|S|', 'Ram|Udbhav|U|', 'Rheinstädter|Maikel C|MC|']
D016229:Amyloid beta-Peptides D001921:Brain D002110:Caffeine D002392:Catechin D002462:Cell Membrane D008856:Microscopy, Fluorescence D056004:Molecular Dynamics Simulation D010446:Peptide Fragments D000077185:Resveratrol D013056:Spectrophotometry, Ultraviolet D014961:X-Ray Diffraction D019207:beta Carotene
resveratrol caffeine β-carotene epigallocatechin gallate Alzheimer's disease cross-β sheets amyloid-β peptides nutrition