ArticleScientific reports2026
Systematic modeling of porphyrin-based photosensitizers for inhibiting Mycobacterium tuberculosis β-Carbonic Anhydrases.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis β-carbonic anhydrases (Mtb-CAs) are zinc-dependent enzymes that play a role in intracellular pH regulation and bacterial physiology within the host. This is because these enzymes are involved in adaptation under hostile conditions, they represent potential molecular targets for anti-tuberculosis research, particularly in the context of drug-resistant strains. In this study, two zinc(II) porphyrin derivatives, AMA01127 and AMA02194, initially designed for anticancer photodynamic therapy, were evaluated for their ability to inhibit the three β-class carbonic anhydrases of Mtb (β-CA1-3) and to explore associated host-pathogen network relationships. Enzymatic assays revealed that AMA02194 selectively inhibited Mtb-CAβ1 and β2 with inhibition constants of 8.2 and 39.7 nM, respectively, and displayed stronger potency than the reference inhibitor acetazolamide under the tested conditions. Docking analyses supported these findings by showing favorable binding of AMA02194 to the zinc-coordinated active site of β-CA1 and β-CA2, stabilized through hydrophobic and polar interactions. AMA01127 demonstrated the strongest docking affinity toward β-CA1 but exhibited comparatively weaker inhibition across isoforms. Network-based systems analysis identified enrichment of biological processes associated with zinc ion binding, peptidase activity, and lipid metabolism. Host gene expression profiling provided a lung-tissue expression context and computationally predicted associations for genes including CTSD, GSTP1, and NFE2L2, which are annotated to immune and redox-related functions. Overall, the results support AMA02194 as an isoform-selective inhibitor of Mtb β-carbonic anhydrases at the enzyme level and provide a computational framework for further investigation of porphyrin-based modulators in tuberculosis-related studies.
Indexed as
Identifiers
What OpenQuestion holds
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 OpenQuestion graph.