Changes in physicochemical properties of proteins, caused by modification with alkylhydroxybenzenes

Nikolaev, Yu. A.; Лойко, Н. Г.; Stepanenko, I. Yu.; Shanenko, E. F.; Martirosova, E. I.; Плакунов, В. К.; Kozlova, A. N.; Borzenkov, I. A.; Korotina, O. A.; Rodin, D. S.; Krupyanskiǐ, Yu. F.; Эль-Регистан, Г. И.

doi:10.1134/s0003683808020038

Cited by 10 publications

(16 citation statements)

References 7 publications

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“…First, the standard substrate, Micrococcus luteus cells of the exponential growth stage, was used. The results for the standard substrate were given in [9] (see Fig. 3b from [9]).…”

Section: Activity Of Lysozymementioning

confidence: 99%

“…The results for the standard substrate were given in [9] (see Fig. 3b from [9]). In this work, colloidal chitin was used as a substrate; pH was 7.4.…”

Section: Activity Of Lysozymementioning

confidence: 99%

“…For a long time, the native structure of proteins has been stabilized using a well known ligand, glycerol [5,6]. In recent years, experimental works appeared in which the action of new biologically active substances, chemical analogues of microbial anabiosis autoinductors such as hexyl and methylre sorcinols [7][8][9][10][11][12][13], on the structural, dynamic, and functional properties of proteins was studied. Alkylre sorcinols are known and are of interest because, at cer tain concentrations, fairly rapidly cause the transition of microbial cells from the vegetative into dormant (anabiotic) state [14,15].…”

Section: Introductionmentioning

confidence: 99%

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Possible mechanisms of the influence of hexylresorcinol on the structure-dynamic and functional properties of lysozyme protein

Krupyanskiǐ

Abdulnasyrov

Лойко

et al. 2012

Russ. J. Phys. Chem. B

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The influence of hexylresorcinol on the structure, equilibrium fluctuations, and functional activ ity of water soluble enzyme lysozyme was studied over a wide range of hexylresorcinol concentrations. Hex ylresorcinol was found to be not only a stabilizer of lysozyme. At low hexylresorcinol concentrations (2 to 10 molecules per lysozyme globule), the activity of lysozyme sharply increased; activity began to decrease as the concentration grew. The influence of hexylresorcinol on the structural, dynamic, and functional lysozyme characteristics is well described by models of preferential hydration and preferential protein interaction with hexylresorcinol. The hexylresorcinol molecule consists of hydrophobic (alkyl radical) and hydrophilic (aro matic nucleus) moieties, which has additional regulatory action on the functional activity of lysozyme. As the concentration of hexylresorcinol increases, the effect of regions with preferential hydration begins to notice ably predominate over the effect of preferential interaction with hexylresorcinol. At hexylresorcinol concen trations higher than 100 molecules per lysozyme globule, the activity of lysozyme is fully inhibited. This is caused by the preferential hydration of the protein with the displacement of hexylresorcinol from direct con tacts with it. The displacement of hexylresorcinol causes the formation of high density hexylresorcinol micelles. Dense micelles interfere with the approach of substrates to the protein and fully inhibit its functional activity. The complete inhibition of lysozyme activity occurs at hexylresorcinol concentrations lower by an order of magnitude than glycerol inhibiting concentrations.

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“…First, the standard substrate, Micrococcus luteus cells of the exponential growth stage, was used. The results for the standard substrate were given in [9] (see Fig. 3b from [9]).…”

Section: Activity Of Lysozymementioning

confidence: 99%

“…The results for the standard substrate were given in [9] (see Fig. 3b from [9]). In this work, colloidal chitin was used as a substrate; pH was 7.4.…”

Section: Activity Of Lysozymementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Possible mechanisms of the influence of hexylresorcinol on the structure-dynamic and functional properties of lysozyme protein

Krupyanskiǐ

Abdulnasyrov

Лойко

et al. 2012

Russ. J. Phys. Chem. B

Self Cite

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“…C7-and C12-alkylhydroxybenzene affected both the degree of protein swelling, viscosity, and the degree of hydrophobicity. The effects depended on the structure of these compounds, their concentration, and the pH of the solution [202].…”

Section: Phenolic Lipids Inhibit Bacterial Fungal Protozoan and Pamentioning

confidence: 99%

Biological activity of phenolic lipids

Stasiuk

Kozubek

2009

Cell. Mol. Life Sci.

228

158

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Phenolic lipids are a very diversified group of compounds derived from mono and dihydroxyphenols, i.e., phenol, catechol, resorcinol, and hydroquinone. Due to their strong amphiphilic character, these compounds can incorporate into erythrocytes and liposomal membranes. In this review, the antioxidant, antigenotoxic, and cytostatic activities of resorcinolic and other phenolic lipids are described. The ability of these compounds to inhibit bacterial, fungal, protozoan and parasite growth seems to depend on their interaction with proteins and/or on their membrane-disturbing properties.

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“…W ostatnich latach wykazano, że niektóre związki z grupy fenoli, a w szczególności alkilohydroksybenzeny, do których należy rezorcyna, są dobrymi regulatorami aktywności lizozymu. Wykazano, że związki te ze względu na swoją chemiczną strukturę oraz rodzaj oddziaływania na cząsteczkę białka, modyfikują lizozym pochodzący z białka jaja kurzego [19,20]. Zmodyfikowany lizozym wykazuje zmiany konformacyjne, obejmujące również centrum aktywne, którym towarzyszą zmiany wła-ściwości fizykochemicznych enzymu.…”

Section: Wyniki I Dyskusjaunclassified

Applying Resorcin as Lysozyme-Protective Agent in the Course of Its High-Temperature Modification

Leśnierowski¹,

Borowiak²

2012

ZNTJ

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GRZEGORZ LEŚNIEROWSKI, ROBERT BOROWIAK  ZASTOSOWANIE REZORCYNY JAKO ŚRODKA OCHRONNEGO LIZOZYMU PODCZAS JEGO WYSOKOTEMPERATUROWEJ MODYFIKACJIS t r e s z c z e n i e Celem niniejszej pracy była ocena rezorcyny jako środka chroniącego lizozym podczas jego wysokotemperaturowej modyfikacji. Analizowano wpływ dodatku tego środka na zmianę aktywności hydrolitycznej zmodyfikowanego enzymu oraz stopień jego oligomeryzacji. Modyfikacja wysokotemperaturowa polegała na oligomeryzacji lizozymu w temperaturze 90 i 95 °C z udziałem substancji utleniającej w postaci H 2 O 2 lub odczynnika Reciclean®. Uzyskane po modyfikacji próby poddano badaniom analitycznym obejmującym oznaczenie aktywności hydrolitycznej enzymu oraz określenie stopnia jego oligomeryzacji.Dzięki zastosowaniu rezorcyny, jako środka chroniącego lizozym podczas jego wysokotemperaturowej modyfikacji, uzyskano efekt 75-procentowej ochrony aktywności hydrolitycznej enzymu. Ponadto obserwowano zwiększony udział oligomerycznych form lizozymu w preparatach uzyskanych po modyfikacji.

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Changes in physicochemical properties of proteins, caused by modification with alkylhydroxybenzenes

Cited by 10 publications

References 7 publications

Possible mechanisms of the influence of hexylresorcinol on the structure-dynamic and functional properties of lysozyme protein

Possible mechanisms of the influence of hexylresorcinol on the structure-dynamic and functional properties of lysozyme protein

Biological activity of phenolic lipids

Applying Resorcin as Lysozyme-Protective Agent in the Course of Its High-Temperature Modification

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