Evidence map›Paper›PMID 27776180›Full record

ArticlePloS one2016

Investigating the Interaction of Fe Nanoparticles with Lysozyme by Biophysical and Molecular Docking Studies.

Zahra Aghili, Saba Taheri, Hojjat Alizadeh Zeinabad, Leila Pishkar, Ali Akbar Saboury, Arash Rahimi, Mojtaba Falahati

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
6.1field-weighted citation impact, top 3% of its field
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

21 citing papers in PubMed, 91 citations in OpenAlex.

  1. Insulin and Human Serum Albumin Interactions with Core-Shell FeThe journal of physical chemistry. B · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Milk Protein Adsorption on Metallic Iron Surfaces.Nanomaterials (Basel, Switzerland) · 2023
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A health concern regarding the protein corona, aggregation and disaggregation.Biochimica et biophysica acta. General subjects · 2019
    Review
  17. Article
  18. Article
  19. Review
  20. 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

7 authors at 4 institutions in 1 country.

Zahra AghiliDepartment of Biology, Islamic Azad University, Science and Research Branch, Tehran, Iran.
Saba TaheriDepartment of Biology, Islamshahr Branch, Islamic Azad University, Islamshahr, Iran.
Hojjat Alizadeh ZeinabadMEMS & NEMS Lab, Department of Electrical and Computer Engineering, University of Tehran, Tehran, Iran.
Leila PishkarYoung Researchers and Elite Club, Islamshahr Branch, Islamic Azad University, Islamshahr, Iran.
Ali Akbar SabouryInstitute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran.
Arash RahimiDepartment of Biology, Islamic Azad University, Science and Research Branch, Tehran, Iran.
Mojtaba FalahatiDepartment of Nanotechnology, Faculty of Advance Science and Technology, Islamic Azad University of Pharmaceutical Sciences (IAUPS), Tehran, Iran.
Islamic Azad University Islamshahr Branch · IRIslamic Azad University, Science and Research Branch · IRUniversity of Tehran · IRIslamic Azad University Pharmaceutical Sciences Branch · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herein, the interaction of hen egg white lysozyme (HEWL) with iron nanoparticle (Fe NP) was investigated by spectroscopic and docking studies. The zeta potential analysis revealed that addition of Fe NP (6.45±1.03 mV) to HEWL (8.57±0.54 mV) can cause to greater charge distribution of nanoparticle-protein system (17.33±1.84 mV). In addition, dynamic light scattering (DLS) study revealed that addition of Fe NP (92.95±6.11 nm) to HEWL (2.68±0.37 nm) increases suspension potential of protein/nanoparticle system (51.17±3.19 nm). Fluorescence quenching studies reveled that both static and dynamic quenching mechanism occur and hydrogen bond and van der Waals interaction give rise to protein-NP system. Synchronous fluorescence spectroscopy of HEWL in the presence of Fe NP showed that the emission maximum wavelength of tryptophan (Trp) residues undergoes a red-shift. ANS fluorescence data indicated a dramatic exposure of hydrophobic residues to the solvent. The considerable reduction in melting temperature (T(m)) of HEWL after addition of Fe NP determines an unfavorable interaction system. Furthermore circular dichoroism (CD) experiments demonstrated that, the secondary structure of HEWL has not changed with increasing Fe NP concentrations; however, some conformational changes occur in tertiary structure of HEWL. Moreover, protein-ligand docking study confirmed that the Fe NP forms hydrogen bond contacts with HEWL.

Indexed as

AnimalsCircular DichroismDynamic Light ScatteringHydrogen BondingIronModels, MolecularMolecular Docking SimulationMuramidaseNanoparticlesProtein Structure, TertiarySpectrometry, Fluorescencehen egg lysozymeIronMuramidase

Identifiers

PMID27776180
PMCPMC5077090
OpenAlexW2538694480

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.