ArticleBMC microbiology2026
Aspergillus flavus glutathione transferase as a potential approach for synthesis of epothilone-glutathione conjugates with enhanced anticancer activity for the drug-resistant cells: characterization and molecular docking analysis.
Article in BMC microbiology, 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
6 authors.
Funding
Abstract
Epothilone is one of the lead anticancer compounds, with unique binding affinity to the cellular β-tubulin, however, the solubility and efficiency towards the drug-resistant tumors are the challenges. Glutathionylation has been recently used as a sophisticated tool to enhance the solubility and efficiency of the bioactive compounds. Consequently, the purpose of this study was to purify and assess the potency glutathione transferase as one-pot approach for glutathione-epothilone complex synthesis. Glutathione transferase (GT) was purified from Aspergillus flavus EFBL-SKH (PV263561) to its homogeneity by ion exchange, and affinity chromatography, with an overall maximum activity 72.22 μmol/mg/min, at 37–42 °C, pH 7.0–7.5, with 28 kDa under SDS-PAGE. The highest affinity (Km) of A. flavus GT was reported for CDNB (0.11 mM), Epothilone (0.31 mM) and MBHC (0.37 mM) as co-substrates with glutathione. The utmost catalytic efficiency (Kcat/Km) were reported for CDNB (13.4 mM−1 s−1), MBHC (2.25 mM−1 s-1) and Epothilone (2.39 mM−1 s−1). The GT mediated reaction of glutathione—epothilone conjugate was purified and checked by LC/MS, with 823.9 m/z. The glutathione-epothilone complex has an elevated molecular flexibility, higher solubility via the stronger interactions with aqueous environments and biological targets, with moderate lipophilicity. From the ESOL Log S values, the solubility of epothilone was increased by 100 folds via glutathione conjugation. From the SwissADME, the accessibility of glutathione-epothilone conjugate was completely diminished as a P-glycoprotein substrate, unlike to the higher feasibility of epothilone, ensuring the molecular structural change of the compound by Glutathionylation. The docking simulation gave a binding affinity -8.0 kcal/ mol for epothilone with the GT binding pocket. The chemical conjugation of glutathione-Epothilone was confirmed from the XRD analysis. The energy of binding of glutathione-epothilone B complex and epothilone with β-tubulin was -7.7–8.0 kcal/mol. The anticancer activity of the glutathione-Epothilone conjugate towards the HepG-2 was 1.9 and 1.45 μM, at molar ratios 1:2 and 1:4 M/M, respectively, by 2.5 higher activity folds, compared to the Epothilone individually. The selectivity indices of GSH-EPT complex was 5.8–6.2 folds, compared to the EPT (2.1- 2.6 folds), to HepG-2 over the normal cells.
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.