ArticleScientific reports2026
Interaction of a biologically active Zn
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
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report the synthesis and characterization of a novel Zn2+ complex derived from a coumarin-based azo dye ligand. The complex was confirmed by 1H NMR and ESI–MS analyses and further examined for its biological activity. Antibacterial assays revealed significant inhibition against Escherichia coli (DH5α), while cytotoxicity tests on the human breast cancer cell line MDA-MB-468 indicated moderate dose-dependent effects. Protein-binding studies using UV–Vis, fluorescence, circular dichroism, and time-resolved fluorescence spectroscopy demonstrated that the complex interacts with human serum albumin (HSA) through a static quenching mechanism, accompanied by conformational changes and a reduction in esterase-like activity. Thermodynamic analysis indicated spontaneous binding driven primarily by hydrogen bonding and van der Waals interactions, which were consistent with molecular docking results showing preferential localization of the ligand at subdomain IB of HSA. Together, these findings highlight the dual biological activity and protein-binding capability of the Zn2+ complex, suggesting its promise as a scaffold for the design of new metal-based therapeutic agents.
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.