Evidence map›Paper›PMID 39656377›Full record

ArticleMolecular diversity2025

Molecular modeling studies, in vitro antioxidant and antimicrobial assay and BSA affinity of novel benzyl-amine derived scaffolds as CYP51B inhibitors.

Jovana S Marjanović, Jovana D Matić, Žiko Milanović, Vera M Divac, Marijana M Kosanić, Miloš R Petković, Marina D Kostić

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Article in Molecular diversity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

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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

7 authors.

Jovana S MarjanovićFaculty of Science, University of Kragujevac, Radoja Domanovića 12, 34000, Kragujevac, Serbia.
Jovana D MatićInstitute for Information Technologies, University of Kragujevac, Jovana Cvijica bb, 34000, Kragujevac, Serbia.
Žiko MilanovićInstitute for Information Technologies, University of Kragujevac, Jovana Cvijica bb, 34000, Kragujevac, Serbia.
Vera M DivacFaculty of Science, University of Kragujevac, Radoja Domanovića 12, 34000, Kragujevac, Serbia.
Marijana M KosanićFaculty of Science, University of Kragujevac, Radoja Domanovića 12, 34000, Kragujevac, Serbia.
Miloš R PetkovićFaculty of Pharmacy, University of Belgrade, Vojvode Stepe 450, 11221, Belgrade, Serbia.
Marina D KostićInstitute for Information Technologies, University of Kragujevac, Jovana Cvijica bb, 34000, Kragujevac, Serbia. marinak@uni.kg.ac.rs.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

New scaffolds derived from benzylamine were prepared, characterized, and tested for their antimicrobial, antioxidant activities and binding interactions with BSA. Structure-activity relationship analysis revealed that compounds incorporating both benzylamine and quinoline or pyridine moieties (specifically 3a and 3d) demonstrated potent antifungal activity, surpassing that of the standard drug Ketoconazole against Penicillium italicum. Molecular docking studies confirmed significant inhibitory activity against the CYP51B enzyme-an essential component of fungal cell walls. In addition, compounds 3h, 3d and 3b displayed promising DPPH radical scavenging activity, indicating its strong potential as an antioxidant source. Thermodynamic parameters of standard antiradical mechanisms confirmed antiradical capacity expressed via formal hydrogen atom transfer (FHT). The results of spectrofluorometric assays and molecular docking studies on the affinity of the tested compounds for the BSA enzyme confirmed that all compounds show significant binding affinity for active site III, with compound 3d demonstrating the highest binding affinity. Key pharmacokinetic parameters were assessed using ADMET analysis, ensuring the viability of these compounds for potential therapeutic applications.

Indexed as

14-alpha Demethylase InhibitorsAntifungal AgentsAnti-Infective AgentsAntioxidantsBenzylaminesSerum Albumin, BovineSterol 14-DemethylaseMicrobial Sensitivity TestsModels, MolecularMolecular Docking SimulationPenicilliumStructure-Activity Relationship14-alpha Demethylase InhibitorsAntifungal AgentsAnti-Infective AgentsAntioxidantsbenzylamineBenzylaminesSerum Albumin, BovineSterol 14-DemethylaseAntimicrobial activityAntioxidant activityBenzylamine derivativesBSA affinityMolecular docking

Identifiers

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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.