Evidence map›Paper›PMID 35684479›Full record

ArticleMolecules (Basel, Switzerland)2022

BSA Interaction, Molecular Docking, and Antibacterial Activity of Zinc(II) Complexes Containing the Sterically Demanding Biomimetic N

Eman Soliman, Mohamed M Ibrahim, Mohamed E El-Khouly, Ibrahim El-Mehasseb, Abd El-Motaleb M Ramadan, Magdy E Mahfouz, Shaban Y Shaban, Rudi van Eldik

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. 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
1.2field-weighted citation impact, top 22% 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

2 citing papers in PubMed, 14 citations in OpenAlex.

  1. IntegrativeFrontiers in pharmacology · 2025
    Article
  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

8 authors at 4 institutions in 4 countries.

Eman SolimanChemistry Department, Faculty of Science, Kafrelsheikh University, Kafrelsheikhheikh 33516, Egypt.
Mohamed M IbrahimChemistry Department, College of Science, Taif University, Taif 21944, Saudi Arabia.
Mohamed E El-KhoulyInstitute of Basic and Applied Sciences, Egypt-Japan University of Science and Technology (E-JUST), Borg El-Arab 21934, Egypt.ORCID 0000-0002-8458-8950
Ibrahim El-MehassebChemistry Department, Faculty of Science, Kafrelsheikh University, Kafrelsheikhheikh 33516, Egypt.
Abd El-Motaleb M RamadanChemistry Department, Faculty of Science, Kafrelsheikh University, Kafrelsheikhheikh 33516, Egypt.ORCID 0000-0002-7643-1144
Magdy E MahfouzZoology Department, Faculty of Science, Kafrelsheikh University, Kafr El Sheikh 33516, Egypt.
Shaban Y ShabanChemistry Department, Faculty of Science, Kafrelsheikh University, Kafrelsheikhheikh 33516, Egypt.ORCID 0000-0003-3717-6803
Rudi van EldikDepartment of Chemistry and Pharmacy, University of Erlangen-Nuremberg, 91058 Erlangen, Germany.ORCID 0000-0003-4271-0118
Kafrelsheikh University · EGEgypt-Japan University of Science and Technology · EGFriedrich-Alexander-Universität Erlangen-Nürnberg · DETaif University · SA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two zinc(II) complexes, DBZ and DBZH4, that have (ZnN3S2) cores and differ in the bridging mode of the ligating backbone, effectively bind to BSA. The binding affinity varies as DBZ > DBZH4 and depends on the ligand structure. At low concentrations, both complexes exhibit dynamic quenching, whereas at higher concentrations they exhibit mixed (static and dynamic) quenching. The energy transfer mechanism from the BSA singlet excited state to DBZ and DBZH4, is highly likely according to steady-state fluorescence and time-correlated singlet photon counting. Molecular docking was used to support the mode of interaction of the complexes with BSA and showed that DBZ had more energy for binding. Furthermore, antibacterial testing revealed that both complexes were active but to a lesser extent than chloramphenicol. In comparison to DBZH4, DBZ has higher antibacterial activity, which is consistent with the binding constants, molecular docking, and particle size of adducts. These findings may have an impact on biomedicine.

Indexed as

Serum Albumin, BovineZincAnti-Bacterial AgentsBinding SitesBiomimeticsLigandsMolecular Docking SimulationProtein BindingSpectrometry, FluorescenceAnti-Bacterial AgentsLigandsSerum Albumin, BovineZincantibacterialassociation affinityenergy transfermetallodrugzinc thiolate

Identifiers

PMID35684479
PMCPMC9182146
OpenAlexW4281642812

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.