Evidence map›Paper›PMID 39648421›Full record

ArticleCurrent protein & peptide science2025

Discovery of Sulfanilamide-diazo Derivatives Incorporating Benzoic Acid Moieties as Novel Inhibitors of Human Carbonic Anhydrase II Activity.

Farshid Belani, Maryam Mehrabi, Hadi Adibi, Masomeh Mehrabi, Reza Khodarahmi

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Article in Current protein & peptide science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed
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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

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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. Dual-target carbonic anhydrase inhibitors in cancer therapy: progress, challenges, and opportunities.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
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4 · The record

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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

5 authors.

Farshid BelaniDepartment of biology, Faculty of Sciences, Razi University, Kermanshah, Iran.
Maryam MehrabiDepartment of biology, Faculty of Sciences, Razi University, Kermanshah, Iran.
Hadi AdibiPharmaceutical Sciences Research Center, Health Institute, Kermanshah University of Medical Sciences, Kermanshah, Iran.
Masomeh MehrabiMedical Biology Research Center, Health Technology Institute, Kermanshah University of Medical Sciences, Kermanshah, Iran.
Reza KhodarahmiMedical Biology Research Center, Health Technology Institute, Kermanshah University of Medical Sciences, Kermanshah, Iran.

Funding

Kermanshah University of Medical Sciences (KUMS) Research Council 4030051
6 · The paper itself

Abstract

backgroundSulfonamides are widely used carbonic anhydrase inhibitors (CAIs) in clinical settings, however, their nonspecific inhibition of multiple carbonic anhydrase isoforms can lead to reduced efficacy and side effects. This study aimed to develop sulfanilamide-diazo derivatives incorporating benzoic acid moieties as novel inhibitors of hCA II activity to reduce side effects and enhance selectivity for different CA isozymes.

methodsWe investigated the interaction between these derivatives and the hCA II isozyme via various spectroscopic and docking methods.

resultsThe kinetic data demonstrates that compound 1 (C1) and compound 2 (C2) share a similar inhibitory strength against hCA II, effectively inhibiting its esterase activity through a noncompetitive mechanism with Ki values at low micromolar levels. Fluorescence measurements indicated that the synthesized compounds suppressed the inherent fluorescence of hCA II via a static quenching process, with each compound showing a singular binding site within the enzyme. Thermodynamic evidences highlight the significance of van der Waals interactions and hydrogen bonding in the binding process. The results of molecular docking indicated that both C1 and C2 effectively obstruct the entrance to hCA II's active site, with no significant differences in their binding conformations.

conclusionWhile C1 and C2 exhibit CA inhibitory potency lower than that of sulfonamide compounds, this study offers valuable insights that could pave the way for the development of a promising scaffold for designing new carbonic anhydrase inhibitors.

Indexed as

Benzoic AcidCarbonic Anhydrase IICarbonic Anhydrase InhibitorsSulfanilamideSulfanilamidesBinding SitesCatalytic DomainHumansHydrogen BondingIsoenzymesKineticsMolecular Docking SimulationProtein BindingStructure-Activity RelationshipThermodynamicsBenzoic AcidCarbonic Anhydrase IICarbonic Anhydrase InhibitorsIsoenzymesSulfanilamideSulfanilamidesCarbonic anhydrase inhibitorscarboxylic acid/sulfonamide compoundsdocking.fluorescencequenchingsynthesis

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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.