Evidence map›Paper›PMID 28097462›Full record

ArticleJournal of fluorescence2017

Thermally Stable Schiff Base and its Metal Complexes: Molecular Docking and Protein Binding Studies.

Umran Duru Kamaci, Musa Kamaci, Aysegul Peksel

Abstract read
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Article in Journal of fluorescence, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Promising Schiff bases in antiviral drug design and discovery.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2023
    Review
  4. Development of Metal Complexes for Treatment of Coronaviruses.International journal of molecular sciences · 2022
    Article
  5. Article
  6. 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

3 authors.

Umran Duru KamaciFaculty of Arts and Sciences, Department of Chemistry, Yıldız Technical University, Esenler, 34220, Istanbul, Turkey.
Musa KamaciFaculty of Sciences and Letters, Department of Chemistry, Piri Reis University, Tuzla, 34940, Istanbul, Turkey. mkamaci@pirireis.edu.tr.
Aysegul PekselFaculty of Arts and Sciences, Department of Chemistry, Yıldız Technical University, Esenler, 34220, Istanbul, Turkey.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this paper, interaction of Schiff base and its metal complexes carrying naphthalene ring in the structure with bovine serum albumin (BSA) were investigated using UV-vis absorption, fluorescence spectroscopies and molecular docking methods. The effect on the binding mechanism and properties of these compounds containing metal-free, iron and copper ions were also investigated. The fluorescence spectroscopy results showed that fluorescence intensity of BSA in the presence of different concentration of ligands was decreased through a static quenching mechanism. Binding constants (KSV, Kbin and Ka) and thermodynamic parameters (ΔG, ΔH and ΔS) for the ligand-protein interactions were also determined. ΔG values of ligand-protein interaction were calculated in the range - 6.3 to -5.5 kcal/mol. These negative values showed that binding process is spontaneous and, hydrogen bonding and van der Waals force were main interaction of the protein and ligands. ΔH and ΔS value were also calculated in the range of 1.10 to 1.26 kJ/mol and 0.133 to 0.135 kJ/mol. K, respectively. These positive values indicated that the binding process between ligands and BSA are endothermic and electrostatic interaction, respectively.

Indexed as

Molecular Docking SimulationAnimalsBinding SitesCattleCoordination ComplexesMetalsProtein BindingSchiff BasesSerum Albumin, BovineSpectrometry, FluorescenceThermodynamicsCoordination ComplexesMetalsSchiff BasesSerum Albumin, BovineBovine serum albuminMetal complexesMolecular dockingProtein bindingThermally stable Schiff base

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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.