Inhibition of the Self-Assembly of Aβ and of Tau by Polyphenols: Mechanistic Studies

The amyloid-β (Aβ) peptide and tau protein are thought to play key neuropathogenic roles in Alzheimer's disease (AD). Both Aβ and tau self-assemble to form the two major pathological hallmarks of AD: amyloid plaques and neurofibrillary tangles, respectively. In this review, we show that natural...

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Bibliographic Details
Published in:	Molecules (Basel, Switzerland) Vol. 24; no. 12; p. 2316
Main Authors:	Zheng, Qiuchen, Kebede, Micheal T, Kemeh, Merc M, Islam, Saadman, Lee, Bethany, Bleck, Stuart D, Wurfl, Liliana A, Lazo, Noel D
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 22-06-2019 MDPI
Subjects:	Alzheimer's disease Amino acids amyloid assemblies Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - metabolism amyloid-β self-assembly Animals Antioxidants Bioavailability Biological effects Cancer Dementia Dementia disorders Drug therapy Enzymes Epigallocatechin-3-gallate Flavonoids Humans Laboratory animals Lipophilic Models, Molecular Molecular Structure neurofibrillary tangles Partial pressure Peptides Phosphorylation Polyphenols Polyphenols - chemistry Polyphenols - pharmacology Protein Aggregates - drug effects Protein Aggregation, Pathological - drug therapy Protein Binding Protein Multimerization - drug effects Proteins Review Self-assembly Structure-Activity Relationship tau hyperphosphorylation Tau protein tau Proteins - chemistry tau Proteins - metabolism tau self-assembly polyphenols tau hyperphosphorylation amyloid-β self-assembly neurofibrillary tangles Alzheimer′s disease tau self-assembly amyloid assemblies
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Summary:	The amyloid-β (Aβ) peptide and tau protein are thought to play key neuropathogenic roles in Alzheimer's disease (AD). Both Aβ and tau self-assemble to form the two major pathological hallmarks of AD: amyloid plaques and neurofibrillary tangles, respectively. In this review, we show that naturally occurring polyphenols abundant in fruits, vegetables, red wine, and tea possess the ability to target pathways associated with the formation of assemblies of Aβ and tau. Polyphenols modulate the enzymatic processing of the amyloid-β precursor protein and inhibit toxic Aβ oligomerization by enhancing the clearance of Aβ42 monomer, modulating monomer-monomer interactions and remodeling oligomers to non-toxic forms. Additionally, polyphenols modulate tau hyperphosphorylation and inhibit tau β-sheet formation. The anti-Aβ-self-assembly and anti-tau-self-assembly effects of polyphenols increase their potential as preventive or therapeutic agents against AD, a complex disease that involves many pathological mechanisms.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23
ISSN:	1420-3049 1420-3049
DOI:	10.3390/molecules24122316