Binding of fluorescent acridine dyes acridine orange and 9-aminoacridine to hemoglobin: Elucidation of their molecular recognition by spectroscopy, calorimetry and molecular modeling techniques

Chatterjee, Sabyasachi; Kumar, Gopinatha Suresh

doi:10.1016/j.jphotobiol.2016.03.045

Cited by 59 publications

(20 citation statements)

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“…9 Also in 2016 many examples of papers making the same claim can be found in the literature. [10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26] These latter references are solely meant as examples of the widespread nature of the backbone uorescence claim and are not an allinclusive list. More importantly, we would like to point out that 3D uorescence spectra are simply one of the many experiments reported in those articles.…”

Section: Introductionmentioning

confidence: 99%

On the purported “backbone fluorescence” in protein three-dimensional fluorescence spectra

et al. 2016

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Section: Introductionmentioning

confidence: 99%

On the purported “backbone fluorescence” in protein three-dimensional fluorescence spectra

et al. 2016

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“…In the case of hemoglobin, the absorption spectra of the heme prosthetic group in hemoglobin is very sensitive to changes in polypeptide environment—structure, oxidation state, and ligand binding, rendering the technique highly suitable to follow Hb-ligand binding (Messori et al, 2006). Typically the hHb spectrum shows two major absorbance in the 199–700 nm range—a peak at ~200 nm due to the CO carbonyl groups in the amino acids and a Soret band seen at 405–450 nm due to the π–π transitions due to the heme moiety embedded in a hydrophobic pocket in the protein backbone (Messori et al, 2006; Chatterjee and Kumar, 2016). Our data (Figure 2) for bovine Hb showed a broad band in the 420–530 nm range, with its peak at 478 nm and a slight shoulder at ~450 nm.…”

Section: Resultsmentioning

confidence: 99%

“…Scientists have studied the interactions of a number azo dyes with proteins like hemoglobin and serum albumin. Changes in protein conformation as a result of protein–dye interaction can lead to change/loss of biological function of the protein, leading to toxicity (Chatterjee and Kumar, 2016). A number of studies show that azo dyes can show genotoxic, mutagenic, and developmental effects.…”

Section: Introductionmentioning

confidence: 99%

A Study of the Interaction of Bovine Hemoglobin with Synthetic Dyes Using Spectroscopic Techniques and Molecular Docking

2017

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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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“…It also acts as a buffer, antioxidant and a transporter of CO 2 , nitric oxide, CNin the blood. The toxicity of food colourants (Chatterjee and Kumar, 2016), pharmaceuticals and nanomaterials (Sekar et al, 2015) have been studied by multi spectroscopic analysis of their binding with hemoglobin molecule. Tetracycline (TC) is a broad spectrum antibiotics used for the treatment of numerous infections in humans and animal husbandry and also as feed additive for animal growth and disease prevention (Chang et al, 2015).…”

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confidence: 99%

Article 31

2019

sfj

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Tetracycline (TC) is a widely used antibiotic for disease prevention and cure in humans and animal husbandry. Its interaction with bovine hemoglobin (BHb) protein is studied in this work to investigate the kinetics, and the potential in vivo toxicity of TC residue in cattle, at different reaction conditions. Spectroscopic measurements of BHb in the presence and absence of TC were carried out via UV/Visible spectrophotometer at different pH, reaction times and TC concentrations. Likewise, the sulphydryl reactivity of the CysF9[93]β sulphydryl groups of the BHb with 5,5'-dithiobis(2-nitrobenzoate), DTNB, was studied at pH 7.2, under pseudo-first order reaction conditions, as an indicator of tertiary and quaternary structural changes of the BHb in the presence and absence of TC. The observed changes in the soret peak of the UV/Visible spectra of the BHb suggest possible conformational and micro environmental changes of the BHb heme moiety with increasing pH, reaction time and TC concentrations. From the kinetic study, the sulphydryl reactivity is shown to be reversible with decrease in the apparent forward second order rate constant, k app , from 11.02 in the absence of TC to 8.358 in the presence of TC. The result obtained shows that there is a possible interaction between BHb and TC with may result to changes in the structure and consequently influence the oxygen binding affinity of BHb.

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Binding of fluorescent acridine dyes acridine orange and 9-aminoacridine to hemoglobin: Elucidation of their molecular recognition by spectroscopy, calorimetry and molecular modeling techniques

Cited by 59 publications

References 53 publications

On the purported “backbone fluorescence” in protein three-dimensional fluorescence spectra

On the purported “backbone fluorescence” in protein three-dimensional fluorescence spectra

A Study of the Interaction of Bovine Hemoglobin with Synthetic Dyes Using Spectroscopic Techniques and Molecular Docking

Article 31

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