ArticleACS omega2022
Inhibition Mechanisms of (-)-Epigallocatechin-3-gallate and Genistein on Amyloid-beta 42 Peptide of Alzheimer's Disease via Molecular Simulations.
Article in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Epigallocatechin Gallate as a State-Dependent Modulator of Amyloid-Biomolecules · 2026Review
- DynamiSpectra: A Python Software Package and Web Platform for Molecular Dynamics Data Analysis in Computational Biology.Journal of chemical information and modeling · 2025Article
- Evaluation of the Sporadic Anti-Alzheimer's Activity of Purpurin Using In Silico, In Vitro, and In Vivo Approaches.Molecular neurobiology · 2025Article
- Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics.Proteins · 2025Review
- In vitro and in silico neuroprotective evaluation of new biotransformation metabolites of (-)-α-bisabolol.Scientific reports · 2025Article
- Epigallocatechin 3-gallate-induced neuroprotection in neurodegenerative diseases: molecular mechanisms and clinical insights.Molecular and cellular biochemistry · 2025Review
- Identification of Chlorogenic Acids fromACS omega · 2025Article
- Article
- Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases.Life (Basel, Switzerland) · 2023Review
- Global Analysis ofMolecules (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The misfolding and self-assembly of amyloid-beta (Aβ) peptides are one of the most important factors contributing to Alzheimer's disease (AD). This study aims to reveal the inhibition mechanisms of (-)-epigallocatechin-3-gallate (EGCG) and genistein on the conformational changes of Aβ42 peptides by using molecular docking and molecular dynamics (MD) simulation. The results indicate that both EGCG and genistein have inhibitory effects on the conformational transition of Aβ42 peptide. EGCG and genistein reduce the ratio of β-sheet secondary structures of Aβ42 peptide while inducing random coil structures. In terms of hydrophobic interactions in the central hydrophobic core of Aβ42 peptide, the binding affinities of EGCG are significantly larger in comparison with that of genistein. Our findings illustrate the inhibition mechanisms of EGCG and genistein on the Aβ42 peptides and prove that EGCG is a very promising inhibitor in impeding the conformational change of Aβ42 peptide.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.