Evidence map›Paper›PMID 35642135›Full record

ArticleChemistryOpen2022

Supramolecular Arrangement and DFT analysis of Zinc(II) Schiff Bases: An Insight towards the Influence of Compartmental Ligands on Binding Interaction with Protein.

Megha Sen Chowdhury, Selcuk Gumus, Sanchari Dasgupta, Ishani Majumder, Abir Bhattacharya, Debasis Das, Jayanta Mukhopadhyay, Debosreeta Bose, Saumya Dasgupta, Yuksel Akinay and 1 more

Open access · goldAbstract read
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In one paragraph

Article in ChemistryOpen, 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
0.8field-weighted citation impact, top 26% 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, 8 citations in OpenAlex.

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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

11 authors at 4 institutions in 4 countries.

Megha Sen ChowdhuryDepartment of Chemistry, Amity Institute of Applied Sciences (AIAS), Amity University, 700156, Kolkata, India.ORCID 0000-0003-4995-9012
Selcuk GumusVan Yuzuncu Yil University, Department of Chemistry, Faculty of Science, 4445065, Van, Turkey.ORCID 0000-0002-8628-8943
Sanchari DasguptaDepartment of Chemistry, University of Calcutta, 92, A. P. C. Road, 700 009, Kolkata, West Bengal, India.ORCID 0000-0003-4997-5258
Ishani MajumderDepartment of Chemistry, University of Calcutta, 92, A. P. C. Road, 700 009, Kolkata, West Bengal, India.ORCID 0000-0002-3085-1303
Abir BhattacharyaDepartment of Physics, The Bhawanipur Education Society College, University of Calcutta, 700020, Kolkata, India.ORCID 0000-0002-5243-8835
Debasis DasDepartment of Chemistry, University of Calcutta, 92, A. P. C. Road, 700 009, Kolkata, West Bengal, India.ORCID 0000-0003-4570-7168
Jayanta MukhopadhyayEnergy Materials & Devices Division, CSIR-Central Glass and Ceramic Research Institute, 700 032, Kolkata, India.ORCID 0000-0001-7936-5093
Debosreeta BoseDepartment of Chemistry, Amity Institute of Applied Sciences (AIAS), Amity University, 700156, Kolkata, India.ORCID 0000-0001-8429-4779
Saumya DasguptaDepartment of Chemistry, Amity Institute of Applied Sciences (AIAS), Amity University, 700156, Kolkata, India.ORCID 0000-0003-2995-6324
Yuksel AkinayVan Yuzuncu Yil University, Department of Mining, Engineering Faculty, 4445065, Vancity, Turkey.ORCID 0000-0002-6171-6307
Madhumita MukhopadhyayDepartment of Chemistry, Amity Institute of Applied Sciences (AIAS), Amity University, 700156, Kolkata, India.ORCID 0000-0003-0637-5113
University of Calcutta · INAmity University · AEVan Yüzüncü Yıl Üniversitesi · TRCentral Glass and Ceramic Research Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report, for the first time, a detailed crystallographic study of the supramolecular arrangement for a set of zinc(II) Schiff base complexes containing the ligand 2,6-bis((E)-((2-(dimethylamino)ethyl)imino)methyl)-4-R-phenol], where R=methyl/tert-butyl/chloro. The supramolecular study acts as a pre-screening tool for selecting the compartmental ligand R of the Schiff base for effective binding with a targeted protein, bovine serum albumin (BSA). The most stable hexagonal arrangement of the complex [Zn-Me] (R=Me) stabilises the ligand with the highest FMO energy gap (ΔE=4.22 eV) and lowest number of conformations during binding with BSA. In contrast, formation of unstable 3D columnar vertebra for [Zn-Cl] (R=Cl) tend to activate the system with lowest FMO gap (3.75 eV) with highest spontaneity factor in molecular docking. Molecular docking analyses reported in terms of 2D LigPlot+ identified site A, a cleft of domains IB, IIIA and IIIB, as the most probable protein binding site of BSA. Arg144, Glu424, Ser428, Ile455 and Lys114 form the most probable interactions irrespective of the type of compartmental ligands R of the Schiff base whereas Arg185, Glu519, His145, Ile522 act as the differentiating residues with ΔG=-7.3 kcal mol

Indexed as

Schiff BasesZincLigandsMolecular Docking SimulationProtein BindingSerum Albumin, BovineLigandsSchiff BasesSerum Albumin, BovineZinccompartmental liganddensity functional theorymolecular dockingSchiff basesupramolecular arrangement

Identifiers

PMID35642135
PMCPMC9156808
OpenAlexW4281622504

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

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.