Evidence map›Paper›PMID 38766654›Full record

ArticleInternational journal of nanomedicine2024

Biosynthesis of Nanoparticles with Green Tea for Inhibition of β-Amyloid Fibrillation Coupled with Ligands Analysis.

Mai Zhang, Yan Li, Chunli Han, Shiying Chu, Peng Yu, Wenbo Cheng

Abstract read
In one paragraph

Article in International journal of nanomedicine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

6 authors.

Mai ZhangMass Spectrometry Application Center, Tianjin Guoke Medical Technology Development Co., Ltd, Tianjin, People's Republic of China.ORCID 0000-0002-3292-9979
Yan LiMass Spectrometry Application Center, Tianjin Guoke Medical Technology Development Co., Ltd, Tianjin, People's Republic of China.
Chunli HanMass Spectrometry Application Center, Shandong CAS Intelligent Manufacturing Medical Device Technology Co., Ltd, Zaozhuang, People's Republic of China.
Shiying ChuMass Spectrometry Application Center, Tianjin Guoke Medical Technology Development Co., Ltd, Tianjin, People's Republic of China.
Peng YuMass Spectrometry Application Center, Tianjin Guoke Medical Technology Development Co., Ltd, Tianjin, People's Republic of China.
Wenbo ChengMass Spectrometry Application Center, Tianjin Guoke Medical Technology Development Co., Ltd, Tianjin, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Inhibition of amyloid β protein fragment (Aβ) aggregation is considered to be one of the most effective strategies for the treatment of Alzheimer's disease. (-)-Epigallocatechin-3-gallate (EGCG) has been found to be effective in this regard; however, owing to its low bioavailability, nanodelivery is recommended for practical applications. Compared to chemical reduction methods, biosynthesis avoids possible biotoxicity and cumbersome preparation processes. Materials and Methods: The interaction between EGCG and Aβ42 was simulated by molecular docking, and green tea-conjugated gold nanoparticles (GT-Au NPs) and EGCG-Au NPs were synthesized using EGCG-enriched green tea and EGCG solutions, respectively. Surface active molecules of the particles were identified and analyzed using various liquid chromatography-tandem triple quadrupole mass spectrometry methods. ThT fluorescence assay, circular dichroism, and TEM were used to investigate the effect of synthesized particles on the inhibition of Aβ42 aggregation. Results: EGCG as well as apigenin, quercetin, baicalin, and glutathione were identified as capping ligands stabilized on the surface of GT-Au NPs. They more or less inhibited Aβ42 aggregation or promoted fibril disaggregation, with EGCG being the most effective, which bound to Aβ42 through hydrogen bonding, hydrophobic interactions, etc. resulting in 39.86% and 88.50% inhibition of aggregation and disaggregation effects, respectively. EGCG-Au NPs were not as effective as free EGCG, whereas multiple thiols and polyphenols in green tea accelerated and optimized heavy metal detoxification. The synthesized GT-Au NPs conferred the efficacy of diverse ligands to the particles, with inhibition of aggregation and disaggregation effects of 54.69% and 88.75%, respectively, while increasing the yield, enhancing water solubility, and decreasing cost. Conclusion: Biosynthesis of nanoparticles using green tea is a promising simple and economical drug-carrying approach to confer multiple pharmacophore molecules to Au NPs. This could be used to design new drug candidates to treat Alzheimer's disease.

Indexed as

Amyloid beta-PeptidesMetal NanoparticlesPeptide FragmentsAlzheimer DiseaseCamellia sinensisCatechinGoldHumansLigandsMolecular Docking SimulationProtein AggregatesAmyloid beta-Peptidesamyloid beta-protein (1-42)Catechinepigallocatechin gallateGoldLigandsPeptide FragmentsProtein Aggregatesamyloid β protein(-)-epigallocatechin-3-gallategold nanoparticlesgreen synthesisgreen tealiquid chromatography tandem triple quadrupole mass spectrometry

Identifiers

PMID38766654
PMCPMC11102095

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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.