ArticleFrontiers in chemistry2016
A Study of the Interaction of Bovine Hemoglobin with Synthetic Dyes Using Spectroscopic Techniques and Molecular Docking.
Article in Frontiers in chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 32 citations in OpenAlex.
- Gentamicin Targeting Human Hemoglobin Induces Methemoglobin Formation and Decreases Oxygen Affinity: A Molecular Mechanism of Hematologic Toxicity.International journal of molecular sciences · 2026Article
- Spermine: A Hemoglobin Modifier That Reduces Autoxidation and Regulates Oxygen Delivery.International journal of molecular sciences · 2026Article
- Hemoglobin as a pseudoperoxidase and drug target for oxidative stress-related diseases.Signal transduction and targeted therapy · 2025Article
- Comparative Evaluation of UV-Vis Spectroscopy-Based Approaches for Hemoglobin Quantification: Method Selection and Practical Insights.Biomolecules · 2024Article
- Inhibitory effects of thymol and carvacrol on heme degradation and oxidative products due to tartrazine:Heliyon · 2024Article
- Inspirations of Biomimetic Affinity Ligands: A Review.ACS omega · 2022Review
- PCR inhibition in qPCR, dPCR and MPS-mechanisms and solutions.Analytical and bioanalytical chemistry · 2020Review
- A biophysical probe on the binding of 2-mercaptothioazoline to bovine hemoglobin.Environmental science and pollution research international · 2019Article
- Inhibition mechanisms of hemoglobin, immunoglobulin G, and whole blood in digital and real-time PCR.Analytical and bioanalytical chemistry · 2018Article
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synthetic dyes are a very efficient class of dyes that are ingested or come into contact with the skin from numerous sources (cosmetics, textiles, leather, paper, and drugs). An important component of their safety profile is the interactions that they form after they enter the body. Hemoglobin is a functionally important protein that can form multiple interactions with soluble compounds present in the blood, and hence forms an important aspect of the toxicological or safety profile of the dyes. Here we study the interaction between bovine hemoglobin and organic dyes using UV-Vis absorbance and fluorescence spectroscopy. Molecular modeling was used to visualize the binding site and partners of the dye molecules, within the hemoglobin molecule. We find that all four dyes studied form sufficiently strong interactions with hemoglobin to allow for the formation of potentially toxic interactions. Molecular modeling showed that all four dyes bind within the central cavity of the hemoglobin molecule. However, binding partners could not be identified as multiple binding conformations with very similar energies were possible for each dye.
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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.