Conformation changes of albumin in its interaction with physiologically active compounds as studied by quasi-elastic light scattering spectroscopy and ultrasonic method

Hushcha, T. O.; Luik, A. I.; Naboka, Yu. N.

doi:10.1016/s0039-9140(00)00454-9

Cited by 77 publications

(35 citation statements)

References 7 publications

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“…ALP and total protein levels on other hand are related to the function of hepatic cell. Increase in serum level of ALP is due to increased synthesis, in presence of increasing biliary pressure [40].…”

Section: Discussionmentioning

confidence: 99%

Can Malachite Green Concentrations Cause Hepatic Toxic Effects in Adult Albino Rats: Histological, Biochemical and Immunohistochemical

NAM¹,

Elgendy²

2016

J Cytol Histol

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Malachite green (MG) has been widely used as the most efficacious antifungal agent in the fish farming industry. The aim of this study is to evaluate hepatotoxicity of different MG concentrations in adult albino rats. Forty five adult male albino rats were equally divided into 3 groups, each contains 15 rats. Group I (control), Group II (received daily dose of 3ug/kg b.wt of MG by oral gavage): divided into three subgroup equally according to time of taken sample and Group III (received daily gavage dose of 60ug/kg b.wt of MG by oral gavage): divided into three subgroup equally according to time of taken sample (Samples were taken 2 and 4 weeks from the start of the experiment and 2 weeks after drug stoppage (wash out). Hepatotoxicity was evaluated by biochemical, histopathological and immunohistochemical study. MG caused an increase of alanine aminotransferase, aspartate amino transferase (ALT and AST), alkaline phosphatase (ALP) levels, and decrease in total protein in animals treated with MG as compared to control. These biochemical alterations were confirmed by the presence of different histological changes as degeneration of hepatocytes with congested dilated central vein , mononuclear inflammatory cells infiltration with significant increase in caspase-3 expression with decrease in survivin expression and this changes were highly significant in rats treated with higher doses than other groups and persist even after 2 weeks from MG stoppage .We can conclude that MG and its residues in the edible tissue of fish could not be ignored due to their suspected hepatotoxicity with apoptotic changes even at lower doses. This leads us to put strict limitations on its use in the fish farming industry in Egypt.

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Section: Discussionmentioning

confidence: 99%

Can Malachite Green Concentrations Cause Hepatic Toxic Effects in Adult Albino Rats: Histological, Biochemical and Immunohistochemical

NAM¹,

Elgendy²

2016

J Cytol Histol

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“…Year 2015 | Volume 3 | Issue 3 | Page 291-307 excretion of those organic molecules/dyes can be greatly influenced due to binding with serum proteins [7] Moreover, there is indication of conformational modification due to binding with small dyes and drugs, which tends to change secondary and tertiary structures [8].…”

Section: Canadian Chemical Transactionsmentioning

confidence: 99%

“…It was assumed that ERS interacted with BSA and formed ERS-BSA complex. The binding number (m) and equilibrium constant (β) of the binding reaction can be deduced as follows: BSA+ m.DYE ↔ BSA-m.DYE (8) The equilibrium constant was deduced as follows:…”

Section: Stoichiometry Of the Azo Dyes-bsa And Adenine Systemmentioning

confidence: 99%

Study of the Binding of Thiazolyazoresorcinol and Thiazolyazocresol Dyes with BSA and Adenine by Spectral, Electrochemical and Molecular Docking Methods

2016

Can Chem Trans

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Abstract:Interaction of thiazolyazoresorcinol (TAR) and thiazolyazocresol (TAC) with bovine serum albumin (BSA) and DNA base (adenine) were investigated by UV-visible, fluorescence, ATR -IR spectroscopy, cyclic voltammetry and molecular docking methods. The results studied by ATR-IR indicate that the secondary structures of the protein have been changed by the interaction of TAR and TAC with BSA. After the addition of TAR and TAC solution into BSA and adenine, the oxidative peak currents increased with the negatively shift of the peak potential and no appearance of new peak. The results from electrochemical studies suggested that the response of TAR and TAC at glassy carbon electrode was a diffuse controlled irreversible process. The results of molecular docking calculation clarify the binding mode and the binding sites which are in good accordance with the experiment results and hydrophobic force play a major role in the binding.

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“…These changes appear to affect the secondary and tertiary structure of albumin. Hushcha et al (15) reported that albumin globules have the most compact configuration at physiological pH, and either increasing the pH of the medium to 8.0 or decreasing it to 5.4 resulted in the increase of globule size. The interaction with CPZ causes conformational changes of albumin similar to basic transitions.…”

mentioning

confidence: 99%

“…Binding of anionic ligands results in a more compact structure, and binding of cationic ligands apparently results in an increase in the overall volume of albumin (9). On the other hand, Hushcha et al (15) reported that binding of CPZ to albumin is able per se to cause conformational changes in protein similar to basic transitions.…”

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confidence: 99%

Quenching of the intrinsic fluorescence of bovine serum albumin by chlorpromazine and hemin

Silva

Cortez

Louro

2004

Braz J Med Biol Res

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The binding of chlorpromazine (CPZ) and hemin to bovine serum albumin was studied by the fluorescence quenching technique. CPZ is a widely used anti-psychotic drug that interacts with blood components, influences bioavailability, and affects function of several biomolecules. Hemin is an important ferric residue of hemoglobin that binds within the hydrophobic region of albumin with high specificity. Quenching of the intrinsic fluorescence of bovine serum albumin (BSA) was observed by selectively exciting tryptophan residues at 290 nm. Emission spectra were recorded in the range from 300 to 450 nm for each quencher addition. Stern-Volmer graphs were plotted, and the quenching constant estimated for BSA solution titrated with hemin at 25ºC was 1.44 (± 0.05) x 10 5 M -1 . Results showed that bovine albumin tryptophans are not equally accessible to CPZ, in agreement with the idea that polar or charged quenchers have more affinity for amino acid residues on the outer wall of the protein. Hemin added to albumin solution at a molar ratio of 1:1 quenched about 25% of their fluorescence. The quenching effect of CPZ on albumin-hemin solution was stronger than on pure BSA. This increase can be the result of combined conformational changes in the structure of albumin caused firstly by hemin and then by CPZ. Our results suggest that the primary binding site for hemin on bovine albumin may be located asymmetrically between the two tryptophans along the sequence formed by subdomains IB and IIA, closer to tryptophan residue 212.

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Conformation changes of albumin in its interaction with physiologically active compounds as studied by quasi-elastic light scattering spectroscopy and ultrasonic method

Cited by 77 publications

References 7 publications

Can Malachite Green Concentrations Cause Hepatic Toxic Effects in Adult Albino Rats: Histological, Biochemical and Immunohistochemical

Can Malachite Green Concentrations Cause Hepatic Toxic Effects in Adult Albino Rats: Histological, Biochemical and Immunohistochemical

Study of the Binding of Thiazolyazoresorcinol and Thiazolyazocresol Dyes with BSA and Adenine by Spectral, Electrochemical and Molecular Docking Methods

Quenching of the intrinsic fluorescence of bovine serum albumin by chlorpromazine and hemin

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