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Updated: May 30, 2026
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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
Published on: May 22, 2018
Apple Procyanidins Suppress Amyloid β-Protein Aggregation
Toshihiko Toda1, Tadahiro Sunagawa, Tomomasa Kanda
1Molecular Gerontology, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015, Japan.
Biochemistry Research International
|August 10, 2011
Summary
Apple polyphenols, specifically procyanidins (PCs), show neuroprotective effects. These compounds significantly inhibit amyloid-beta (Aβ) aggregation and reduce Aβ-induced neurotoxicity, suggesting potential for Alzheimer's disease treatment.
Area of Science:
- * Biochemistry and Molecular Biology
- * Neuroscience
- * Gerontology
Background:
- * Procyanidins (PCs) are key apple polyphenols (APs) with previously demonstrated lifespan-extending properties in *C. elegans*.
- * Amyloid-beta (Aβ) protein aggregation is a central pathological feature of Alzheimer's disease (AD).
Purpose of the Study:
- * To investigate the potential neuroprotective effects of PCs.
- * To evaluate the anti-aggregative activity of PCs on Aβ aggregation.
- * To assess the impact of PCs on Aβ-induced neurotoxicity and cell proliferation.
Main Methods:
- * In vitro assessment of PC's effect on Aβ42 aggregation and dissociation.
- * Evaluation of PC's inhibition of Aβ42 neurotoxicity in PC-12 cells.
- * Measurement of PC's effect on cell proliferation in PC-12 cells.
Main Results:
- * PCs significantly suppressed Aβ42 aggregation in a dose-dependent manner.
- * PCs effectively dissociated pre-formed Aβ42 aggregates.
- * PCs demonstrated significant inhibition of Aβ42 neurotoxicity and stimulated proliferation in PC-12 cells.
Conclusions:
- * Procyanidins are potent inhibitors and disaggregators of Aβ42 aggregation.
- * PCs exhibit significant neuroprotective properties against Aβ-induced toxicity.
- * Apple polyphenols and procyanidins show promise as neuroprotective factors against Alzheimer's disease pathology.
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Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...