Evidence map›Paper›PMID 41551223›Full record

ArticleIET nanobiotechnology2026

Mechanistic Insights Into Protein Aggregation Inhibition by Green-Synthesized Silver Nanoparticles: A Study on Human Lysozyme.

Md Tauqir Alam, Mohd Ahmar Rauf, Arman Khan, Rizwan Hussain

Abstract read
In one paragraph

Article in IET nanobiotechnology, 2026. 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. Review
  2. Article
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

4 authors.

Md Tauqir AlamDepartment of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India, amu.ac.in.ORCID https://orcid.org/0000-0002-3085-5945
Mohd Ahmar RaufDepartment of Biotechnology, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India, amu.ac.in.ORCID https://orcid.org/0000-0001-5639-2208
Arman KhanDepartment of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India, amu.ac.in.
Rizwan HussainDepartment of Industrial Chemistry, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India, amu.ac.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A characteristic of many neurodegenerative disorders, such as Parkinson's and Alzheimer's, is amyloidogenic protein aggregation, for which there are currently no proven cures. Aging, mutation, and physiological stress can cause proteins to deviate from their natural folding patterns, potentially leading to the formation of hazardous protein aggregates. Noble metal nanoparticles (NPs), due to their unique physicochemical properties, have emerged as promising tools in biomedicine, with applications ranging from tissue engineering to drug delivery and diagnostics. Although concerns regarding cytotoxicity exist, small-sized silver (Ag) NPs (AgNPs) have demonstrated potential in antiviral, anticancer, and antibacterial therapies. This study investigated the development of biocompatible AgNPs using a green synthesis approach and examined their chaperone-like activity against protein aggregation, emphasizing the role of meticulous in vitro design. Human lysozyme (HLZ) served as a model protein for aggregation inhibition assays. Biogenic AgNPs exhibited a concentration-dependent effect on HLZ aggregation, demonstrating an optimal inhibitory concentration, followed by a decrease in efficacy at higher concentrations. Furthermore, astrocytes treated with AgNPs displayed reduced protein aggregation, suggesting a chaperone-like behavior. The initial phase focused on the detailed characterization of AgNPs synthesized using orange juice extract. Subsequently, this study explored the mechanistic understanding of AgNP-mediated inhibition of protein aggregation under controlled conditions. A battery of biophysical techniques, including circular dichroism (CD), 8-anilino-1-naphthalene-sulfonic acid (ANS) fluorescence, thioflavin T (ThT) fluorescence, Congo red (CR) assay, and turbidity measurements, was employed to meticulously assess the inhibitory effect on HLZ aggregation in vitro.

Indexed as

Green Chemistry TechnologyMetal NanoparticlesMuramidaseProtein AggregatesSilverBenzothiazolesCongo RedHumansBenzothiazolesCongo RedMuramidaseProtein AggregatesSilverCongo redhuman lysozymeprotein aggregationsilver nanoparticlesthioflavin T

Identifiers

PMID41551223
PMCPMC12809263

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.