ArticleMolecular diversity2024
Novel fluoroquinolones analogues bearing 4-(arylcarbamoyl)benzyl: design, synthesis, and antibacterial evaluation.
Article in Molecular diversity, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 3 citations in OpenAlex.
- Biodesulfurization and activation of a thionated levofloxacin derivative: antimicrobial evaluation and LC-MS-based metabolic profiling.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Design, Synthesis, andPharmaceuticals (Basel, Switzerland) · 2025Article
- Investigation of bacterial DNA gyrase Inhibitor classification models and structural requirements utilizing multiple machine learning methods.Molecular diversity · 2024Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial resistance to fluoroquinolone has been increasing at an alarming rate worldwide. In an attempt to find more potent anti-bacterial agents, an efficient, straightforward protocol was performed to obtain a large substrate scope of novel ciprofloxacin and sarafloxacin analogues conjugated with 4-(arylcarbamoyl)benzyl 7a-ab. All prepared compounds were evaluated for their anti-bacterial activities against three gram-positive strains (Methicillin resistant staphylococcus aureus (MRSA), Staphylococcus aureus, and Enterococcus faecalis) as well as three gram-negative strains (Pseudomonas aeruginosa, Klebsiella pneumonia, and Escherichia coli) through three standard methods including broth microdilution, agar-disc diffusion, and agar-well diffusion assays. Most of the compounds exhibited great to excellent anti-bacterial potencies against MRSA and S. aureus. Among the targeted compounds, derivative 7n exhibited great antibacterial potency, which was noticeably more potent than parent ciprofloxacin. Subsequently, a molecular docking study was performed for this compound to find out its probable binding mode with the active site of S. aureus DNA gyrase (PDB ID: 2XCT).
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Registered trials
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 Socratic graph.