Evidence map›Paper›PMID 40628933›Full record

ArticleScientific reports2025

Inhibitory mechanisms of amentoflavone on amyloid-β peptide aggregation revealed by replica exchange molecular dynamics.

Suxia Wu, Chang Liu, Yang Li, Xiaoyu Zhang, Qianji Han, Heng Zhao, Kun Zhao, Yaru Dang, Ruihan Wang, Shitao Song

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Suxia WuHebei Normal University of Science and Technology, Qinhuangdao, 066600, Hebei, PR China.
Chang LiuHebei Normal University of Science and Technology, Qinhuangdao, 066600, Hebei, PR China.
Yang LiHebei Normal University of Science and Technology, Qinhuangdao, 066600, Hebei, PR China.
Xiaoyu ZhangDepartment of Digital Information, Hebei Institute of International Business and Economics, Qinhuangdao, 066311, Hebei, PR China.
Qianji HanHebei Normal University of Science and Technology, Qinhuangdao, 066600, Hebei, PR China.
Heng ZhaoHebei Normal University of Science and Technology, Qinhuangdao, 066600, Hebei, PR China.
Kun ZhaoHebei Normal University of Science and Technology, Qinhuangdao, 066600, Hebei, PR China.
Yaru DangHebei Normal University of Science and Technology, Qinhuangdao, 066600, Hebei, PR China. dangyr4058@hevttc.edu.cn.
Ruihan WangHebei Normal University of Science and Technology, Qinhuangdao, 066600, Hebei, PR China. ruihwang@163.com.
Shitao SongHebei Normal University of Science and Technology, Qinhuangdao, 066600, Hebei, PR China. sst1210@163.com.

Funding

Science Research Project of Hebei Education Department QN2025083
6 · The paper itself

Abstract

Amyloid-β (Aβ) aggregation is a central pathological hallmark of Alzheimer's disease, with soluble trimers recognized as particularly neurotoxic species. Amentoflavone (AMF), a natural biflavonoid compound, has shown strong inhibitory effects on Aβ aggregation. However, its underlying molecular mechanism remains poorly understood. In this study, we employed replica exchange molecular dynamics (REMD) and molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) method to elucidate the interaction between AMF and Aβ peptides. Our results reveal that AMF preferentially binds to the

Indexed as

Amyloid beta-PeptidesBiflavonoidsMolecular Dynamics SimulationProtein AggregatesHumansHydrophobic and Hydrophilic InteractionsProtein Aggregation, PathologicalProtein BindingamentoflavoneAmyloid beta-PeptidesBiflavonoidsProtein AggregatesAggregation Inhibition mechanismAmentoflavoneAmyloid-β aggregationMolecular dynamics simulationVirtual screening

Identifiers

PMID40628933
PMCPMC12238462

What OpenQuestion holds

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Registered trials

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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.