ArticleJournal of fluorescence2025
Elucidating the Binding Mechanism of Kojic Acid with Human Hemoglobin by Molecular Docking and Multi-Spectroscopic Techniques.
Article in Journal of fluorescence, 2025. 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
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kojic acid (KA) is a natural secondary metabolite that is widely known for its skin-lightening properties and also used as food preservative. Here, we have explored the binding and interaction of KA with human hemoglobin (HHb), a multifunctional and the predominant protein in erythrocytes, using multi-spectroscopic techniques, enzymatic activities (esterase and peroxidase) and molecular docking method. The ultraviolet-visible absorption spectra of HHb showed hyperchromic effect at 275 nm upon addition of KA. The fluorescence experiments showed that KA quenches HHb fluorescence and alters the microenvironment around tryptophan residues. The fluorescence quenching mechanism is of static type and there is a single KA binding site on each HHb tetramer. KA binds spontaneously and interacts with HHb through ground state complex formation. The negative values of thermodynamic parameters ([Formula: see text]= -0.010 kcal mol
Indexed as
Identifiers
40788557What 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.