Author
U. Chaudhuri
Bio: U. Chaudhuri is an academic researcher from University of Calcutta. The author has contributed to research in topics: Physics & Myoglobin. The author has an hindex of 4, co-authored 6 publications receiving 164 citations.
Papers
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TL;DR: Binding of chlorpromazine with human hemoglobin has been studied by equilibrium dialysis and fluorescence quenching and results revealed that the binding was positively cooperative with overall affinity constant K = 3.8 x 10(3) M-1.
102 citations
TL;DR: Binding modalities of chlorpromazine and trifluoperazine, two widely used antipsychotic phenothiazine drugs with hemoglobin and myoglobin have been studied to understand how the quaternary, tertiary and secondary structural organisations of the proteins regulate the binding process.
40 citations
TL;DR: The interaction of chlorpromazine (CPZ), a widely used antipsychotic tranquillizer, with the allosteric protein haemoglobin, has been studied by different methods and the possible nature of the binding site of the protein has been discussed on the basis of the information obtained from fluorescence measurements.
12 citations
TL;DR: The extent of oxygen release from two heme proteins, haemoglobin and myoglobin, have been studied in the presence of trifluoperazine and chlorpromazine (5–1000 μM).
Abstract: The extent of oxygen release from two heme proteins, haemoglobin and myoglobin have been studied in the presence of trifluoperazine and chlorpromazine (5–1000 μM).
At a molar ratio (drug: protein) of 1.5, the release of oxygen from haemoglobin was 4 and 15% in the presence of chlorpromazine and trifluoperazine respectively, while from myoglobin the corresponding values were 20 and 40%.
The findings were attributed to the greater extent of local conformational change around tryptophan moieties of each of the proteins induced by trifluoperazine.
10 citations
3 citations
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TL;DR: The synchronous fluorescence, CD and three-dimensional fluorescence spectral results showed that the hydrophobicity of amino acid residues increased and the losing of α-helix content in the presence of PAAB revealed that the microenvironment and conformation of BSA were changed in the binding reaction.
Abstract: In this paper, the interaction between p-aminoazobenzene (PAAB) and BSA was investigated mainly by fluorescence quenching spectra, circular dichroism (CD) and three-dimensional fluorescence spectra under simulative physiological conditions. It was proved that the fluorescence quenching of BSA by PAAB was mainly a result of the formation of a PAAB-BSA complex. The modified Stern-Volmer quenching constant Ka and the corresponding thermodynamic parameters ΔH, ΔG and ΔS at different temperatures were calculated. The results indicated that van der Waals interactions and hydrogen bonds were the predominant intermolecular forces in stabilizing the complex. The distance r = 4.33 nm between the donor (BSA) and acceptor (PAAB) was obtained according to Forster’s non-radioactive energy transfer theory. The synchronous fluorescence, CD and three-dimensional fluorescence spectral results showed that the hydrophobicity of amino acid residues increased and the losing of α-helix content (from 63.57 to 51.83%) in the presence of PAAB. These revealed that the microenvironment and conformation of BSA were changed in the binding reaction.
334 citations
TL;DR: In this article, the adsorption of cytochrome c onto a range of different mesoporous silicates (MPS) was studied, with the pore diameter of the material, which was measured by N2 gas adaption, being crucial to mesopore penetration.
Abstract: The adsorption of cytochrome c onto a range of different mesoporous silicates (MPS) was studied. The materials used, templated using both cationic and nonionic surfactants, have average pore-size diameters in the range from 28 to 130 A. Cytochrome c was found to bind to all MPS investigated, with the pore diameter of the material, which was measured by N2 gas adsorption, being crucial to mesopore penetration. The adsorption of a range of proteins with isoelectric points between 1 and 10 was investigated. For adsorption to occur, the surface charges of the protein and of the MPS must be complementary, in addition to the requirement that the pore diameter be sufficiently large. Pepsin at pH 6.5, for example, is negatively charged and does not adsorb onto cyano-modified silicate whereas subtilisin, which is of a similar size and bears an overall positive charge, is adsorbed. Using resonance Raman spectroscopy, cytochrome c was observed to occur in both high spin and low spin states, in contrast to that in solution, where the protein is predominantly in the low spin state. The presence of the high spin state may account for the enhanced peroxidative activity of the adsorbed protein.
251 citations
TL;DR: Results suggest that the primary binding site for methyl parathion on albumin is close to tryptophan residues 214 of human serum albumin and 212 of bovine serum albumIn, and suggest that this pesticide is potentially toxic for both vertebrates and invertebrates.
204 citations
TL;DR: Histopathology and several blood parameters indicated that oral administrations of nanoparticles were free from toxicity and suggested that polymeric formulations were quite effective for oral delivery of the flavonoid as a therapeutic agent in the treatment of dyslipidemia, hyperglycemia and haemoglobin iron-mediated oxidative stress in type 1 diabetic model.
144 citations
TL;DR: It is demonstrated that in the presence of H(2)O(2), HbA(1c) degrades DNA and protein more efficiently than Hb a(0) and formation of carbonyl content, an index of oxidative stress, is higher by H bA( 1c).
111 citations