Studies of oxidant-induced changes in albumin transport function with a fluorescent probe K-35. Effect of hypochlorite

Азизова, О. А.; Aseychev, A. V.; Beckman, E. M.; Москвина, С.Н.; Skotnikova, O. I.; Смолина, Н. В.; Gryzunov, Yu. A.; Dobretsov, G. E.

doi:10.1007/s10517-012-1613-z

Cited by 8 publications

(7 citation statements)

References 12 publications

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“…It has bactericidal activity but it has become apparent that collateral damage to host tissues is a key event in a number of human pathologies linked with inflammation. − Rate constants , for reaction of hypochlorite with individual biological components have shown that proteins are by far the major targets for hypochlorite in plasma, and HSA, as the most abundant protein, is thought to be the most probable target in general. Oxidatively modified forms of HSA have indeed been detected in several pathological conditions characterized by oxidative stress, and the characterization of model systems of oxidized HSA has mainly been addressed through chemical essays or mass spectrometry methods to quantify and identify chemical modifications induced by hypochlorite, ,− as well as by detecting spectral variations in UV absorption and fluorescence spectroscopy. − …”

Section: Introductionmentioning

confidence: 99%

Structural Response of Human Serum Albumin to Oxidation: Biological Buffer to Local Formation of Hypochlorite

et al. 2016

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The most abundant plasma protein, human serum albumin (HSA), plays a key part in the body's antioxidant defense against reactive species. This study was aimed at correlating oxidant-induced chemical and structural effects on HSA. Despite the chemical modification induced by the oxidant hypochlorite, the native shape is preserved up to oxidant/HSA molar ratio <80, above which a structural transition occurs in the critical range 80-120. This conformational variation involves the drifting of one of the end-domains from the rest of the protein and corresponds to the loss of one-third of the α-helix and a net increase of the protein negative charge. The transition is highly reproducible suggesting that it represents a well-defined structural response typical of this multidomain protein. The ability to tolerate high levels of chemical modification in a folded or only partially unfolded state, as well as the stability to aggregation, provides albumin with optimal features as a biological buffer for the local formation of oxidants.

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Section: Introductionmentioning

confidence: 99%

Structural Response of Human Serum Albumin to Oxidation: Biological Buffer to Local Formation of Hypochlorite

et al. 2016

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“…The content of carbonyl products was measured as described previously with modifications [ 56 ]. The reaction mixtures (200 µL) were composed of 50 µmol·L −1 HSA and 500 µmol·L −1 Tau-NBr 2 or 1000 µmol·L −1 Tau-NHCl in 10 mmol·L −1 PBS at 25 °C and incubated for 1 h; then, 1000 µmol·L −1 methionine was added to scavenge the remaining oxidants.…”

Section: Methodsmentioning

confidence: 99%

Oxidative Alteration of Trp-214 and Lys-199 in Human Serum Albumin Increases Binding Affinity with Phenylbutazone: A Combined Experimental and Computational Investigation

Bertozo

Neto

Ximenes

2018

IJMS

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Human serum albumin (HSA) is a target for reactive oxygen species (ROS), and alterations of its physiological functions caused by oxidation is a current issue. In this work, the amino-acid residues Trp-214 and Lys-199, which are located at site I of HSA, were experimentally and computationally oxidized, and the effect on the binding constant with phenylbutazone was measured. HSA was submitted to two mild oxidizing reagents, taurine monochloramine (Tau-NHCl) and taurine dibromamine (Tau-NBr2). The oxidation of Trp-214 provoked spectroscopic alterations in the protein which were consistent with the formation of N′-formylkynurenine. It was found that the oxidation of HSA by Tau-NBr2, but not by Tau-NHCl, provoked a significant increase in the association constant with phenylbutazone. The alterations of Trp-214 and Lys-199 were modeled and simulated by changing these residues using the putative oxidation products. Based on the Amber score function, the interaction energy was measured, and it showed that, while native HSA presented an interaction energy of −21.3 kJ/mol, HSA with Trp-214 altered to N′-formylkynurenine resulted in an energy of −28.4 kJ/mol, and HSA with Lys-199 altered to its carbonylated form resulted in an energy of −33.9 kJ/mol. In summary, these experimental and theoretical findings show that oxidative alterations of amino-acid residues at site I of HSA affect its binding efficacy.

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“…During the exper iments, dye concentrations in solutions were varied in a range of (1-5) × 10 -6 mol/L; equal volumes of MNPs and protein containing samples were placed into a cell with a dye solution. The degrees of the probe-protein interaction in different samples were comparatively estimated in terms of effective protein concentration (c eff , %), which is equal to the fluores cence intensity ratio between probe-protein com plexes in MNPs containing and MNPs free (refer ence) samples [26].…”

Section: Methodsmentioning

confidence: 99%

Study of protein coatings cross-linked via the free-radical mechanism on magnetic nanoparticles by the method of spectral and fluorescent probes

et al. 2014

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2) interaction between two tyrosyl radicals: P 1 tyr • + P 2 tyr • → P 1 tyr-tyrP 2 , Abstract-Magnetite nanoparticles have been obtained with stable coatings formed from bovine and human serum albumins. The coatings are fixed by free radical cross linking of the proteins with the use of their abil ity to form interchain covalent bonds under the action of free radicals, which are generated with participation of transition metals present on nanoparticle surface. The method of spectral and fluorescent probes has been employed for the first time to describe the properties of coatings with the use of various dyes. It has been shown that, when studying the adsorption and free radical cross linking of proteins on nanoparticles, it is reasonable to use polymethine and squarylium dyes for estimating the functional properties of the proteins forming the coatings. It has been found that as many as 50% of molecules forming an albumin coating cross linked via the free radical mechanism retain their capability of bonding to a fluorescent dye. It has been con cluded that the proteins occurring in the structure of the coatings retain their functional properties.

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Studies of oxidant-induced changes in albumin transport function with a fluorescent probe K-35. Effect of hypochlorite

Cited by 8 publications

References 12 publications

Structural Response of Human Serum Albumin to Oxidation: Biological Buffer to Local Formation of Hypochlorite

Structural Response of Human Serum Albumin to Oxidation: Biological Buffer to Local Formation of Hypochlorite

Oxidative Alteration of Trp-214 and Lys-199 in Human Serum Albumin Increases Binding Affinity with Phenylbutazone: A Combined Experimental and Computational Investigation

Study of protein coatings cross-linked via the free-radical mechanism on magnetic nanoparticles by the method of spectral and fluorescent probes

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