Evidence map›Paper›PMID 39485531›Full record

ArticleNaunyn-Schmiedeberg's archives of pharmacology2025

Unveiling the interaction, cytotoxicity and antibacterial potential of pyridine derivatives: an experimental and theoretical approach with bovine serum albumin.

Rosalin Das, Patitapaban Mohanty, Pragyan P Dash, Swagatika Mishra, Ajit K Bishoyi, Lokanath Mishra, Laxmipriya Prusty, Devi P Behera, Debasmita Dubey, Monalisa Mishra and 4 more

Abstract read
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In one paragraph

Article in Naunyn-Schmiedeberg's archives of pharmacology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

14 authors.

Rosalin DasSchool of Biotechnology, Gangadhar Meher University, Sambalpur, Odisha, 768001, India.
Patitapaban MohantyDepartment of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, Odisha, 768018, India.
Pragyan P DashDepartment of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, Odisha, 768018, India.
Swagatika MishraDepartment of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, Odisha, 768018, India.
Ajit K BishoyiDepartment of Clinical Hematology, Institute of Medical Sciences and SUM Hospital, Siksha 'O' Anusandhan Deemed University, Bhubaneswar, Odisha, 751003, India.
Lokanath MishraDepartment of Life Science, National Institute of Technology, Rourkela, 769008, India.
Laxmipriya PrustyDepartment of Chemistry, National Institute of Technology, Rourkela, 769008, India.
Devi P BeheraDepartment of Chemistry, National Institute of Technology, Rourkela, 769008, India.
Debasmita DubeyMedical Research Laboratory, Institute of Medical Sciences and SUM Hospital, Siksha 'O' Anusandhan Deemed University, Bhubaneswar, Odisha, 751003, India.
Monalisa MishraDepartment of Life Science, National Institute of Technology, Rourkela, 769008, India.
Harekrushna SahooDepartment of Chemistry, National Institute of Technology, Rourkela, 769008, India.
Mohd S KhanDepartment of Biochemistry, College of Science, King Saud University, Riyadh, 11451, Saudi Arabia.
Santosh K SethiSchool of Biotechnology, Gangadhar Meher University, Sambalpur, Odisha, 768001, India. sksethi2k@gmail.com.
Bigyan R JaliDepartment of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, Odisha, 768018, India. bigyan.Jali7@gmail.com.

Funding

DST Biotechnology Govt of Odisha ST-BT-MISC-0008-2020-245/STResearch Supporting Project RSP2024R352
6 · The paper itself

Abstract

The binding interactions between bovine serum albumin (BSA) and three pyridine derivatives, i.e., 2-(5-bromopyridin-3-yl) acetic acid (L1), 3-bromo-5-nitropyridine (L2) and 2-chloro-4-nitropyridine (L3), have been carried out using UV-Vis and fluorescence spectroscopic methods. Fluorescence intensity quenching is observed by adding L2 and L3 to the BSA solution. The quenched fluorescence emission is due to the static nature. An isothermal titration calorimetry (ITC) experiment shows the binding ability of L1 with BSA. The binding constants are found to be 7.23 ± 0.32 × 10

Indexed as

Anti-Bacterial AgentsPyridinesSerum Albumin, BovineAnimalsCattleCell SurvivalMicrobial Sensitivity TestsMolecular Docking SimulationProtein BindingThermodynamicsAnti-Bacterial AgentsPyridinesSerum Albumin, BovineAntibacterial activityBSACyclic voltammetryDrosophila activityFluorescence quenchingMolecular docking

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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.