Targeting the heme proteins hemoglobin and myoglobin by janus green blue and study of the dye–protein association by spectroscopy and calorimetry

Abstract

The binding of the phenazinium dye janus green blue (JGB) to two heme proteins, hemoglobin (Hb) and myoglobin (Mb), was studied by biophysical and microcalorimetry techniques.

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

“…This may lead to exposure of HHb to drugs and small molecules present in the plasma leading to interaction. A few reports on ligand-hemoglobin interactions have been published recently [27][28][29][30][31][32][33]. The molecular aspects of the recognition between acridine dyes and HHb and the related thermodynamics are not yet investigated.…”

Interaction of cyanidin-3-O-glucoside with three proteins

“…They play an important role in physiological activities in human bodies, having numerous functions including the transport of oxygen, dispersion of hydrogen peroxide, and are involved in electron transfer reactions (Chen, IkedaSaito, & Shaik, 2008;Cheng, Liu, Bao, & Zou, 2011). Hb picks up oxygen from the tiny blood capillaries at the base of the lungs and carries it along the arteries to the body tissues, and carries CO 2 from the cells to the lungs for removal (Chatterjee & Kumar, 2014). Mb is found mainly in muscle tissues, and receives oxygen from red blood cells and transports it to the mitochondria of the muscle cells, where the oxygen is used in cellular respiration to generate energy.…”

“…Mb is found mainly in muscle tissues, and receives oxygen from red blood cells and transports it to the mitochondria of the muscle cells, where the oxygen is used in cellular respiration to generate energy. Hb is a tetrameric protein comprising of four polypeptide chains: two identical a-chains comprising of 141 amino acid residues each and two identical b-chains made up of 146 amino acid residues, while Mb is a single polypeptide chain protein of 153 amino acids (Chatterjee & Kumar, 2014 Hb and Mb are not strictly plasma proteins, investigations on the interaction of drugs and small molecules with Hb and Mb are of great importance in terms of understanding their pharmacological actions.…”

Comparative Study of Toluidine Blue O and Methylene Blue Binding to Lysozyme and Their Inhibitory Effects on Protein Aggregation

“…This is governed by the postulate that there is a change in the Trp moiety toward the hydrophilic environment exposing more to the solvent site in the case of TBO, and the corresponding blue shift signified the reverse phenomenon for Try moieties in MB. 46 On the other hand, there is less change in the emission maxima when Δλ was set to be 15 nm, indicating that there is little transformation occurred in Tyr moieties. This finding reinforced that binding of TBO and MB with lyz causes the change in polarity around the Trp residues and most likely around Trp-62 and Trp-63.…”