Effect of Bovine Serum Albumin Redox
Status on Its Interaction with Paraoxon as Determined by Molecular Modeling

Belinskaia, Daria A.; Баталова, А. А.; Гончаров, Н. В.

doi:10.1134/s0022093020050063

Cited by 6 publications

(6 citation statements)

References 7 publications

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“…Differences between HSA and BSA are of particular interest; glycation of HSA dramatically reduces its antioxidant activity, while glycation of BSA somewhat enhances its antioxidant properties. These data correlate with the results of computational experiments aimed at studying the effects of the redox status of HSA and BSA on their binding and esterase activities towards paraoxon [ 60 , 61 ]. From an evolutionary and comparative biochemistry/physiology point of view, the following fact seems to be important: the concentration of glucose in the blood plasma of birds is 1.5–2 times higher than in mammals of a similar mass (so-called benign hyperglycemia), but avian albumin (for example, CSA—Chicken Serum Albumin) gets glycated to a lesser extent than BSA, even when albumins have been exposed to increasing glucose concentrations of up to 500 mM in in vitro experiments [ 171 ].…”

Section: Ga: Biomarker and Pathogenetic Factors Of Dmsupporting

confidence: 72%

“…We have previously shown that Sudlow I and Cys34 sites in HSA and BSA molecules mutually influence each other; a change in the conformation of one leads to conformational changes in the other [ 60 , 61 ]. At the same time, in the redox site, the main role in reciprocal regulation is played by amino acid residues Cys34, His39 and Tyr140(139), and their mutual arrangement; the position of the thiol group of the cysteine and the hydroxyl group of the tyrosine relative to the imidazole ring of His39.…”

Section: Transporting Function and Structural Characteristics Of Albumins Of Different Speciesmentioning

confidence: 99%

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Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Belinskaia

Voronina

Шмурак

et al. 2021

IJMS

161

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Being one of the main proteins in the human body and many animal species, albumin plays a decisive role in the transport of various ions—electrically neutral and charged molecules—and in maintaining the colloidal osmotic pressure of the blood. Albumin is able to bind to almost all known drugs, as well as many nutraceuticals and toxic substances, largely determining their pharmaco- and toxicokinetics. Albumin of humans and respective representatives in cattle and rodents have their own structural features that determine species differences in functional properties. However, albumin is not only passive, but also an active participant of pharmacokinetic and toxicokinetic processes, possessing a number of enzymatic activities. Numerous experiments have shown esterase or pseudoesterase activity of albumin towards a number of endogeneous and exogeneous esters. Due to the free thiol group of Cys34, albumin can serve as a trap for reactive oxygen and nitrogen species, thus participating in redox processes. Glycated albumin makes a significant contribution to the pathogenesis of diabetes and other diseases. The interaction of albumin with blood cells, blood vessels and tissue cells outside the vascular bed is of great importance. Interactions with endothelial glycocalyx and vascular endothelial cells largely determine the integrative role of albumin. This review considers the esterase, antioxidant, transporting and signaling properties of albumin, as well as its structural and functional modifications and their significance in the pathogenesis of certain diseases.

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Section: Ga: Biomarker and Pathogenetic Factors Of Dmsupporting

confidence: 72%

Section: Transporting Function and Structural Characteristics Of Albumins Of Different Speciesmentioning

confidence: 99%

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Belinskaia

Voronina

Шмурак

et al. 2021

IJMS

161

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“…The differences between human and bovine albumin are of particular interest: glycation of HSA sharply decreases its antioxidant activity, while glycation of BSA tends to enhance its antioxidant properties. These data correlate with the results of computational experiments aimed at studying the effect of the redox status of HSA and BSA on their binding and esterase activity towards paraoxon [79,80]. According to the data, human and bovine albumins react differently to the oxidation of Cys34 to sulfenic and sulfinic acids.…”

Section: Albumin and Redox Modulationsupporting

confidence: 68%

Serum Albumin

et al. 2020

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Being one of the most abundant proteins in human and other mammals, albumin plays a crucial role in transporting various endogenous and exogenous molecules and maintaining of colloid osmotic pressure of the blood. It is not only the passive but also the active participant of the pharmacokinetic and toxicokinetic processes possessing a number of enzymatic activities. A free thiol group of the albumin molecule determines the participation of the protein in redox reactions. Its activity is not limited to interaction with other molecules entering the blood: of great physiological importance is its interaction with the cells of blood, blood vessels and also outside the vascular bed. This entry contains data on the enzymatic, inflammatory and antioxidant properties of serum albumin.

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“…Since aggregation is caused by ROS formed in aqueous solution under UVI, the authors concluded that the observed differences in HSA protection are due to the radical intercepting properties of these compounds (ascorbic acid turned out to be the most highly effective compound). However, interactions of antioxidants with the protein molecule may also be important, since there is increasing evidence of a lability of the three-dimensional structure of albumin, which permits cooperativity and allosteric modulation in interactions with various substances, usually characteristic of multimeric proteins [ 33 ].…”

Section: Resultsmentioning

confidence: 99%

“…These are areas containing many non-polar amino acids, which form the binding sites for molecules. These sites also provide the enzymatic activity for albumin: esterase (Sudlow site I) and pseudoesterase (irreversible substrate–enzyme binding, Sudlow site II) [ 33 ].…”

Section: Resultsmentioning

confidence: 99%

Effect of Low-Dose Line-Spectrum and Full-Spectrum UV on Major Humoral Components of Human Blood

Sozarukova,

Skachko,

Chilikina

et al. 2023

Molecules

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Ultraviolet blood irradiation (UVBI) is an alternative approach to the treatment of infectious diseases of various pathogeneses. Recently, UVBI has attracted particular interest as a new immunomodulatory method. Experimental studies available in the literature demonstrate the absence of precise mechanisms of the effect of ultraviolet radiation (UV) on blood. Here, we investigated the effect of UV radiation of line-spectrum mercury lamp (doses up to 500 mJ/cm2) traditionally used in UVBI on the major humoral blood components: albumin, globulins and uric acid. Preliminary data on the effect of various doses of UV radiation of full-spectrum flash xenon lamp (doses up to 136 mJ/cm2), a new promising source for UVBI, on the major blood plasma protein, albumin, are presented. The research methodology included spectrofluorimetric analysis of the oxidative modification of proteins and analysis of the antioxidant activity of humoral blood components by chemiluminometry. The effect of UV radiation on albumin caused its oxidative modification and, accordingly, an impairment of the transport properties of the protein. At the same time, UV-modified albumin and γ-globulins acquired pronounced antioxidant properties compared to native samples. Uric acid mixed with albumin did not protect the protein against UV-induced oxidation. The flash full-spectrum UV qualitatively had the same effect on albumin as line-spectrum UV did, but an order of magnitude lower doses were required to achieve comparable effects. The suggested protocol can be used for selecting a safe individual dose for UV therapy.

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Effect of Bovine Serum Albumin Redox Status on Its Interaction with Paraoxon as Determined by Molecular Modeling

Cited by 6 publications

References 7 publications

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Serum Albumin

Effect of Low-Dose Line-Spectrum and Full-Spectrum UV on Major Humoral Components of Human Blood

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