Tyrosine fluorescence probing of the surfactant-induced conformational changes of albumin

Zhdanova, Nadezda G.; Shirshin, Evgeny A.; Maksimov, Eugene G.; Panchishin, I. M.; Saletsky, A. M.; Фадеев, В. В.

doi:10.1039/c4pp00432a

Cited by 52 publications

(36 citation statements)

References 79 publications

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“…Recently sequential conformational changes in BSA upon surfactant binding was demonstrated using Tyr photophysical parameters as an indicator. The authors have proven that Tyr emission in BSA increases in the unfolded state of the protein as a consequence of the interaction with SDS, and this behavior could be explained by the decrease in the intramolecular quenching and the change in the distance between Tyr and certain amino acids, like Trp.…”

Section: Resultsmentioning

confidence: 99%

Influence of pH and micellar systems on the sensitized photo‐oxidation of bovine serum albumin

et al. 2019

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Photosensitized oxidation of bovine serum albumin (BSA), by using perinaphtenone as a sensitizer, has been studied at pH 7.4 and 11. The selected sensitizer does not present ground‐state complexation with BSA and ensures that the mechanism is mediated by O2(1△g). Strong dependence between BSA–O2(1△g) photo‐oxidation and the pH of the medium has been found. The relative oxygen uptake rate (v− △ O2) and the total quenching rate constant (kt) values are higher at pH 11 than pH 7.4. The enhancement in the alkaline condition is due to conformational changes in the protein and the reactivity of tyrosinate anion with O2(1△g). Even when the tendency with the pH in the presence of sodium dodecyl sulfate (SDS) micelles is similar to that observed in homogeneous media, an increment on the kt value is detected. This effect may be attributable to the strong interaction of BSA–SDS, which leads to the protein unfolding and could leave more exposed photo‐oxidizable amino acids. A protective effect against the O2(1△g)‐mediated photo‐oxidation was observed in reverse micelles (RMs) of sodium bis(2‐ethylhexyl)sulfosuccinate (AOT) by comparing the kt values obtained at W = 10 with respect to the one obtain in homogeneous media. The latter could be mainly explained by the modification in the solvent polarity. Also, another important observation was found, the internal pH inside RMs of AOT sensed through tyrosine absorption was independent of the one used for the formation of the water pool. Hence, the kt values observed at both pH, are quite similar.

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Section: Resultsmentioning

confidence: 99%

Influence of pH and micellar systems on the sensitized photo‐oxidation of bovine serum albumin

et al. 2019

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“…The intrinsic fluorescence of a protein is mainly emitted by tryptophan (Trp) and tyrosine (Tyr) residues, of which the fluorescence intensity of Trp is stronger and more sensitive to changes in the micro environment. Hence, Trp is often used as a fluorescent probe to study protein conformation in the solution state …”

Section: Resultsmentioning

confidence: 99%

Synthesis of Tailed Metalloporphyrins Modified with 2‐Chloronicotinic Acid and Interactions with Human Serum Albumin

Wang

Peng

Zhang

et al. 2017

Bulletin Korean Chem Soc

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Two kinds of free‐base tailed porphyrins modified with 2‐chloronicotinic acid and the corresponding Zn porphyrins have been synthesized. They have been characterized by elemental analysis and NMR, UV/Vis, fluorescence spectra, and infrared spectroscopies. Their configurations have been optimized through theoretical calculations. The fluorescence quantum yields were determined by a comparative method. The interactions between the Zn porphyrins and human serum albumin have been studied by means of fluorescence spectra. The experimental results showed that the interaction mechanism involved a combined fluorescence quenching process (static and dynamic quenching) and that the main driving force was hydrophobic in nature. Quenching constants, binding constants, thermodynamic parameters, and binding distances have been determined.

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“…In this study, we have performed the steady state fluorescence of tyrosine residue by exciting the samples at 275 nm and recording the emission in the range of 280 to 400 nm. Although tryptophan quenching is more widely used than tyrosine for determining protein conformation, the interaction of AA with tyrosine residue might alter its microenvironment therefore, studying tyrosine fluorescence would give a good understanding of any change that follows AA binding . The dose‐dependent quenching of tyrosine fluorescence with increasing concentration of AA might be due to the change in tyrosine microenvironment as a result of structural perturbation that occurred in the AA‐IgG molecule because of the formation of Lys‐Lys cross‐linked adduct (2,6‐diamino hexanoic acid{1‐(N′‐[5‐amino‐1‐formyl‐pentyl]‐hydrazino)‐ethyl}‐amide).…”

Section: Discussionmentioning

confidence: 99%

“…Although tryptophan quenching is more widely used than tyrosine for determining protein conformation, the interaction of AA with tyrosine residue might alter its microenvironment therefore, studying tyrosine fluorescence would give a good understanding of any change that follows AA binding. 50,51 The dose-dependent quenching of tyrosine fluorescence with increasing concentration of AA might be due to the change in tyrosine microenvironment as a result of structural perturbation that occurred in the AA-IgG molecule because of the formation of Lys-Lys cross-linked adduct (2,6-diamino hexanoic acid{1-(N 0 -[5-amino-1-formyl-pentyl]-hydrazino)-ethyl}-amide). Human IgG molecule contains approximately 80 lysine residues 24,52 that represents a potential target for AA modification so the quantification of primary amino groups of protein to determine the available free lysine residues might be useful in determining the extent of protein modification by AA.…”

Section: Discussionmentioning

confidence: 99%

Molecular docking explores heightened immunogenicity and structural dynamics of acetaldehyde human immunoglobulin G adduct

et al. 2019

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Acetaldehyde is a metabolite of ethanol, an important constituent of tobacco pyrolysis and the aldehydic product of lipid peroxidation. Acetaldehyde induced toxicity is mainly due to its binding to cellular macromolecules resulting in the formation of stable adducts accompanied by oxidative stress. The aim of this study was to characterize structural and immunological alterations in human immunoglobulin G (IgG) modified with acetaldehyde in the presence of sodium borohydride, a reducing agent. The IgG modifications were studied by various physicochemical techniques such as fluorescence and CD spectroscopy, free amino group estimation, 2,2‐azobis 2‐amidinopropane (AAPH) induced red blood cell hemolysis as well as transmission electron microscopy. Molecular docking was also employed to predict the preferential binding of acetaldehyde to IgG. The immunogenicity of native and acetaldehyde‐modified IgG was investigated by immunizing female New Zealand white rabbits using native and modified IgG as antigens. Binding specificity and cross reactivity of rabbit antibodies was screened by competitive inhibition ELISA and band shift assays. The modification of human IgG with acetaldehyde results in quenching of the fluorescence of tyrosine residues, decrease in free amino group content, a change in the antioxidant property as well as formation of cross‐linked structures in human IgG. Molecular docking reveals strong binding of IgG to acetaldehyde. Moreover, acetaldehyde modified IgG induced high titer antibodies (>1:12800) in the experimental animals. The antibodies exhibited high specificity in competitive binding assay toward acetaldehyde modified human IgG. The results indicate that acetaldehyde induces alterations in secondary and tertiary structure of IgG molecule that leads to formation of neo‐epitopes on IgG that enhances its immunogenicity.

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Tyrosine fluorescence probing of the surfactant-induced conformational changes of albumin

Cited by 52 publications

References 79 publications

Influence of pH and micellar systems on the sensitized photo‐oxidation of bovine serum albumin

Influence of pH and micellar systems on the sensitized photo‐oxidation of bovine serum albumin

Synthesis of Tailed Metalloporphyrins Modified with 2‐Chloronicotinic Acid and Interactions with Human Serum Albumin

Molecular docking explores heightened immunogenicity and structural dynamics of acetaldehyde human immunoglobulin G adduct

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