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ArticleNaunyn-Schmiedeberg's archives of pharmacology2024

Antibacterial and cytotoxicity studies of pyrrolo-based organic scaffolds and their binding interaction with bovine serum albumin.

Rosalin Das, Pragyan P Dash, Ajit K Bishoyi, Patitapaban Mohanty, Lokanath Mishra, Laxmipriya Prusty, Chita R Sahoo, Rabindra N Padhy, Monalisa Mishra, Harekrushna Sahoo and 3 more

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In one paragraph

Article in Naunyn-Schmiedeberg's archives of pharmacology, 2024. 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

13 authors.

Rosalin DasSchool of Biotechnology, Gangadhar Meher University, Sambalpur, 768001, Odisha, India.
Pragyan P DashDepartment of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, 768018, Odisha, India.
Ajit K BishoyiCentral Research Laboratory, Institute of Medical Sciences and SUM Hospital, Siksha 'O' Anusandhan Deemed University, Bhubaneswar, 751003, Odisha, India.
Patitapaban MohantyDepartment of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, 768018, Odisha, India.
Lokanath MishraDepartment of Life Science, National Institute of Technology, Rourkela, 769008, India.
Laxmipriya PrustyDepartment of Chemistry, National Institute of Technology, Rourkela, 769008, India.
Chita R SahooCentral Research Laboratory, Institute of Medical Sciences and SUM Hospital, Siksha 'O' Anusandhan Deemed University, Bhubaneswar, 751003, Odisha, India.
Rabindra N PadhyCentral Research Laboratory, Institute of Medical Sciences and SUM Hospital, Siksha 'O' Anusandhan Deemed University, Bhubaneswar, 751003, Odisha, India.
Monalisa MishraDepartment of Life Science, National Institute of Technology, Rourkela, 769008, India.
Harekrushna SahooDepartment of Chemistry, National Institute of Technology, Rourkela, 769008, India.
Suban K SahooDepartment of Chemistry, SV National Institute of Technology, Surat, 395007, Gujarat, India.
Santosh K SethiSchool of Biotechnology, Gangadhar Meher University, Sambalpur, 768001, Odisha, India. sksethi2k@gmail.com.
Bigyan R JaliDepartment of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, 768018, Odisha, India. bigyan.Jali7@gmail.com.

Funding

DST Biotechnology Govt Of Odisha ST-BT-MISC-0008-2020-245/ST
6 · The paper itself

Abstract

Two pyrrolo-based compounds, 1H-pyrrolo[3,2-b]pyridine-3-carboxylic acid (L1) and 1H-pyrrolo[3,2-c]pyridine-4-carboxylic acid (L2), were employed for the detection of bovine serum albumin (BSA) by UV-Vis and fluorescence spectroscopic methods in phosphate buffer solution (pH = 7). In the presence of L1 and L2, the fluorescence emission of BSA at 340 nm was quenched and concomitantly a red-shifted emission band appeared at 420 nm (L1)/450 nm (L2). The fluorescence spectral changes indicate the protein-ligand complex formation between BSA and L1/L2. An isothermal titration calorimetry (ITC) experiment was conducted to determine the binding ability between BSA and L1/L2. The binding constants are found to be 4.45 ± 0.22 × 10

Indexed as

Anti-Bacterial AgentsPyrrolesSerum Albumin, BovineAnimalsEscherichia coliGram-Positive BacteriaMicrobial Sensitivity TestsMolecular Docking SimulationProtein BindingPyridinesThermodynamicsAnti-Bacterial AgentsPyridinesPyrrolesSerum Albumin, BovineAntibacterial activityBSADNA gyraseDrosophilaFluorescence quenching

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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.