2020
DOI: 10.1016/j.neurobiolaging.2020.04.012
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Resveratrol-mediated cleavage of amyloid β1–42 peptide: potential relevance to Alzheimer's disease

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Cited by 40 publications
(16 citation statements)
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“…Several natural products have been reported to be able to target these two phenylalanine residues and interact with Aβ through hydrogen bonds or hydrophobic interactions to destroy the normal structure of Aβ fibrils and block its toxicity in AD. Examples of these natural products include the polyphenol stilbene compound resveratrol that can decrease the formation of Aβ plaques [ 133 ], the major compound from the Sappan wood brazilin that can prevent abnormal Aβ aggregation [ 134 ], the polyphenol compound curcumin that interacts with F19 and F20 in the hydrophobic core domain of Aβ and disrupts their β-sheet structure to alleviate their toxicity [ 135 ], a polyphenol compound tannic acid that can stack with the hydrophobic domain of Aβ to prevent their polymerization into fibrils [ 136 ], destabilize the conformation of Aβ fibrils and promote the depolymerization of Aβ [ 137 ], and a group of polycyclic polyphenols theaflavin that binds to the hydrophobic core domain and hydrophobic C-terminus of Aβ to prevent the formation of toxic Aβ aggregates and induce the remodeling of misfolded Aβ aggregates [ 138 ].…”
Section: Neuroprotective Mechanisms Of Natural Products For Admentioning
confidence: 99%
“…Several natural products have been reported to be able to target these two phenylalanine residues and interact with Aβ through hydrogen bonds or hydrophobic interactions to destroy the normal structure of Aβ fibrils and block its toxicity in AD. Examples of these natural products include the polyphenol stilbene compound resveratrol that can decrease the formation of Aβ plaques [ 133 ], the major compound from the Sappan wood brazilin that can prevent abnormal Aβ aggregation [ 134 ], the polyphenol compound curcumin that interacts with F19 and F20 in the hydrophobic core domain of Aβ and disrupts their β-sheet structure to alleviate their toxicity [ 135 ], a polyphenol compound tannic acid that can stack with the hydrophobic domain of Aβ to prevent their polymerization into fibrils [ 136 ], destabilize the conformation of Aβ fibrils and promote the depolymerization of Aβ [ 137 ], and a group of polycyclic polyphenols theaflavin that binds to the hydrophobic core domain and hydrophobic C-terminus of Aβ to prevent the formation of toxic Aβ aggregates and induce the remodeling of misfolded Aβ aggregates [ 138 ].…”
Section: Neuroprotective Mechanisms Of Natural Products For Admentioning
confidence: 99%
“…In addition, curcumin and its derivatives can pass the BBB and have neuroprotective effects against mitochondrial dysfunction, damage, and nitrosative stress [ 46 ]. Moreover, resveratrol significantly decreased the Aβ -42 peptide toxicity toward SH-SY5Y cells that resulted in the cleavage of Aβ 1-42 peptides into smaller fragments [ 110 ]. Metabolism of flavan-3-ols by GM result in various arylvaleric acid, and aryl-γ-valerolactone derivatives that can selectively detoxify Aβ oligomers and prevent AD symptoms in mice [ 111 ].…”
Section: Polyphenolsmentioning
confidence: 99%
“…Resveratrol has been shown to exhibit anti-cancer, anti-inflammatory, anti-aging, cardioprotective and anti-oxidant properties. 93,94 Also, it has anti-amyloidogenic effects and could inhibit the formation and extension of neurotoxic Aβ fibrils. 95 A cell line study by Vingtdeux et al studied the potential effect of resveratrol in AD.…”
Section: Phytochemicalsmentioning
confidence: 99%