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Analysis of interactions between proteins and small-molecule drugs by a biosensor based on a graphene field-effect transistor / S. Xu, T. Wang, G. Liu [et al.] // Sens Actuators, B Chem. - 2021. - Vol. 326. - Ст. 128991, DOI 10.1016/j.snb.2020.128991 . - ISSN 0925-4005
Кл.слова (ненормированные):
Binding kinetics -- FET -- Imatinib -- LMW drugs -- Single-crystal graphene -- Biosensors -- Biosynthesis -- Drug interactions -- Graphene -- Graphene transistors -- Proteins -- Single crystals -- Graphene field-effect transistors -- Graphene sheets -- Interaction kinetics -- Linear response -- Low molecular weight drugs -- Real time -- Small-molecule drugs -- Target proteins -- Field effect transistors
Аннотация: We synthesized large-area single-crystal graphene sheets to use them in biosensors based on field-effect transistors (FET) for quantitative analysis of interaction kinetics and affinity between the imatinib drug and its target protein kinase Abl1. The G-FET biosensor showed an excellent performance and recognized imatinib at as low as 15.5 fM. The biosensor also showed a linear response to the logarithm of imatinib concentration in the 0.1 pM-10 ?M range. This graphene-based FET biosensor (G-FET) was also applied to quantify Abl1 Y253 F mutation and Abl1 dependency on Mg2+ to bind to imatinib in real-time. Results demonstrated in this work clearly showed that the novel G-FET biosensors are very promising to analyze interactions between proteins and low molecular weight drugs. © 2020 Elsevier B.V.

Scopus
Держатели документа:
Shandong Key Laboratory of Biophysics, Institute of Biophysics, Dezhou University, Dezhou, 253023, China
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Collaborative Innovation Center of Light Manipulations and Applications, Shandong Normal University, Jinan, 250358, China

Доп.точки доступа:
Xu, S.; Wang, T.; Liu, G.; Cao, Z.; Frank, L. A.; Jiang, S.; Zhang, C.; Li, Z.; Krasitskaya, V. V.; Li, Q.; Sha, Y.; Zhang, X.; Liu, H.; Wang, J.

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Analysis of interactions between proteins and small-molecule drugs by a biosensor based on a graphene field-effect transistor / S. C. Xu, T. J. Wang, G. F. Liu [et al.] // Sens. Actuator B-Chem. - 2021. - Vol. 326. - Ст. 128991, DOI 10.1016/j.snb.2020.128991. - Cited References:66. - We are grateful for financial support from the Taishan Scholars Program of Shandong Province (tsqn201812104), the Qingchuang Science and Technology Plan of Shandong Province (2019KJJ017 and 2020KJC004), the National Natural Science Foundation of China (61671107, 62071085, 11704059, and 31802309), and the Youth Innovation Team Lead-Education Project of Shandong Educational Committee. . - ISSN 0925-4005

РУБ Chemistry, Analytical + Electrochemistry + Instruments & Instrumentation
Рубрики:
LABEL-FREE DETECTION
CHEMICAL-VAPOR-DEPOSITION
DNA HYBRIDIZATION
Кл.слова (ненормированные):
Single-crystal graphene -- FET -- Binding kinetics -- LMW drugs -- Imatinib
Аннотация: We synthesized large-area single-crystal graphene sheets to use them in biosensors based on field-effect transistors (FET) for quantitative analysis of interaction kinetics and affinity between the imatinib drug and its target protein kinase Abl1. The G-FET biosensor showed an excellent performance and recognized imatinib at as low as 15.5 fM. The biosensor also showed a linear response to the logarithm of imatinib concentration in the 0.1 pM-10 mu M range. This graphene-based FET biosensor (G-FET) was also applied toquantify Abl1 Y253 F mutation and Abl1 dependency on Mg2+ to bind to imatinib in real-time. Results demonstrated in this work clearly showed that the novel G-FET biosensors are very promising to analyze interactions between proteins and low molecular weight drugs.

WOS
Держатели документа:
Dezhou Univ, Inst Biophys, Shandong Key Lab Biophys, Dezhou 253023, Peoples R China.
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Shandong Normal Univ, Collaborat Innovat Ctr Light Manipulat & Applicat, Jinan 250358, Peoples R China.

Доп.точки доступа:
Xu, Shicai; Wang, Tiejun; Liu, Guofeng; Cao, Zanxia; Frank, Ludmila A.; Jiang, Shouzhen; Zhang, Chao; Li, Zhenhua; Krasitskaya, Vasilisa V.; Li, Qiang; Sha, Yujie; Zhang, Xiumei; Liu, Huilan; Wang, Jihua; Taishan Scholars Program of Shandong Province [tsqn201812104]; Qingchuang Science and Technology Plan of Shandong Province [2019KJJ017, 2020KJC004]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [61671107, 62071085, 11704059, 31802309]; Youth Innovation Team Lead-Education Project of Shandong Educational Committee

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Mechanisms of Viscous Media Effects on Elementary Steps of Bacterial Bioluminescent Reaction / A. E. Lisitsa, L. A. Sukovatyi, S. I. Bartsev [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 16. - Ст. 8827, DOI 10.3390/ijms22168827. - Cited References:59. - The research was funded by the Ministry of Science and Higher Education of the Russian Federation (projects No. FSRZ-2020-0006); by RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science (project No. 20-44-243002); by RFBR according to the research project No. 20-34-90118. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
FLAVIN INTERMEDIATE
   REDUCED FLAVIN
   RATE CONSTANTS
   LUCIFERASE
Кл.слова (ненормированные):
bacterial luciferase -- non-steady-state reaction kinetics -- viscosity -- diffusion limitation
Аннотация: Enzymes activity in a cell is determined by many factors, among which viscosity of the microenvironment plays a significant role. Various cosolvents can imitate intracellular conditions in vitro, allowing to reduce a combination of different regulatory effects. The aim of the study was to analyze the media viscosity effects on the rate constants of the separate stages of the bacterial bioluminescent reaction. Non-steady-state reaction kinetics in glycerol and sucrose solutions was measured by stopped-flow technique and analyzed with a mathematical model developed in accordance with the sequence of reaction stages. Molecular dynamics methods were applied to reveal the effects of cosolvents on luciferase structure. We observed both in glycerol and in sucrose media that the stages of luciferase binding with flavin and aldehyde, in contrast to oxygen, are diffusion-limited. Moreover, unlike glycerol, sucrose solutions enhanced the rate of an electronically excited intermediate formation. The MD simulations showed that, in comparison with sucrose, glycerol molecules could penetrate the active-site gorge, but sucrose solutions caused a conformational change of functionally important alpha Glu175 of luciferase. Therefore, both cosolvents induce diffusion limitation of substrates binding. However, in sucrose media, increasing enzyme catalytic constant neutralizes viscosity effects. The activating effect of sucrose can be attributed to its exclusion from the catalytic gorge of luciferase and promotion of the formation of the active site structure favorable for the catalysis.

WOS
Держатели документа:
Siberian Fed Univ, Biophys Dept, Svobodny 79, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Akad Gorodok 50-50, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Lisitsa, Albert E.; Sukovatyi, Lev A.; Bartsev, Sergey, I; Deeva, Anna A.; Kratasyuk, Valentina A.; Nemtseva, Elena, V; Nemtseva, Elena; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science [20-44-243002]; RFBRRussian Foundation for Basic Research (RFBR) [20-34-90118]

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Development of Cellular and Enzymatic Bioluminescent Assay Systems to Study Low-Dose Effects of Thorium / O. V. Kolesnik, T. V. Rozhko, M. A. Lapina [et al.] // Bioengineering-Basel. - 2021. - Vol. 8, Is. 12. - Ст. 194, DOI 10.3390/bioengineering8120194. - Cited References:77 . - ISSN 2306-5354

РУБ Biotechnology & Applied Microbiology + Engineering, Biomedical

Кл.слова (ненормированные):
bioassay -- bioluminescence -- luminous bacteria -- enzymes -- reactive oxygen -- species -- thorium -- low-dose exposure -- radiation hormesis
Аннотация: Thorium is one of the most widespread radioactive elements in natural ecosystems, along with uranium, it is the most important source of nuclear energy. However, the effects of thorium on living organisms have not been thoroughly studied. Marine luminescent bacteria and their enzymes are optimal bioassays for studying low-dose thorium exposures. Luminescent bioassays provide a quantitative measure of toxicity and are characterized by high rates, sensitivity, and simplicity. It is known that the metabolic activity of bacteria is associated with the production of reactive oxygen species (ROS). We studied the effects of thorium-232 (10(-11)-10(-3) M) on Photobacterium phosphoreum and bacterial enzymatic reactions; kinetics of bacterial bioluminescence and ROS content were investigated in both systems. Bioluminescence activation was revealed under low-dose exposures (<0.1 Gy) and discussed in terms of "radiation hormesis". The activation was accompanied by an intensification of the oxidation of a low-molecular reducer, NADH, during the enzymatic processes. Negative correlations were found between the intensity of bioluminescence and the content of ROS in bacteria and enzyme systems; an active role of ROS in the low-dose activation by thorium was discussed. The results contribute to radioecological potential of bioluminescence techniques adapted to study low-intensity radioactive exposures.

WOS
Держатели документа:
RAS, Krasnoyarsk Sci Ctr SB, Inst Biophys SB, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Biophys Dept, Krasnoyarsk 660041, Russia.
Krasnoyarsk State Med Acad, Krasnoyarsk 660022, Russia.
Natl Res Tomsk Polytech Univ, Tomsk 634050, Russia.

Доп.точки доступа:
Kolesnik, Olga V.; Rozhko, Tatiana V.; Lapina, Maria A.; Solovyev, Vladislav S.; Sachkova, Anna S.; Kudryasheva, Nadezhda S.; Kolesnik, Olga

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Specific Activities of Hydromedusan Ca2+-Regulated Photoproteins / N. P. Malikova, E. V. Eremeeva, D. V. Gulnov [et al.] // Photochem. Photobiol. - 2021, DOI 10.1111/php.13556 . - Article in press. - ISSN 0031-8655
Аннотация: Nowadays the recombinant Ca2+-regulated photoproteins originating from marine luminous organisms are widely applied to monitor calcium transients in living cells due to their ability to emit light on Ca2+ binding. Here we report the specific activities of the recombinant Ca2+-regulated photoproteins—aequorin from Aequorea victoria, obelins from Obelia longissima and Obelia geniculata, clytin from Clytia gregaria and mitrocomin from Mitrocoma cellularia. We demonstrate that along with bioluminescence spectra, kinetics of light signals and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of bioluminescent reactions. The highest specific activities were found for obelins and mitrocomin, whereas those of aequorin and clytin were shown to be lower. To determine the factors influencing the variations in specific activities the fluorescence quantum yields for Ca2+-discharged photoproteins were measured and found to be quite different varying in the range of 0.16–0.36. We propose that distinctions in specific activities may result from different efficiencies of singlet excited state generation and different fluorescence quantum yields of coelenteramide bound within substrate-binding cavity. This in turn may be conditioned by variations in the amino acid environment of the substrate-binding cavities and hydrogen bond distances between key residues and atoms of 2-hydroperoxycoelenterazine. © 2021 American Society for Photobiology

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Malikova, N. P.; Eremeeva, E. V.; Gulnov, D. V.; Natashin, P. V.; Nemtseva, E. V.; Vysotski, E. S.

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Thermomechanical analysis of isora nanofibril incorporated polyethylene nanocomposites / C. Jose, C. H. Chan, T. Winie [et al.] // Polym. - 2021. - Vol. 13, Is. 2. - Ст. 299. - P1-15, DOI 10.3390/polym13020299 . - ISSN 2073-4360
Кл.слова (ненормированные):
Avrami model -- Crystallization -- Mechanical properties -- Polymer-cellulose nanocomposites -- Aliphatic compounds -- Cellulose nanocrystals -- Crystallization kinetics -- Fillers -- Nanocomposites -- Nanofibers -- Polyethylenes -- Viscoelasticity -- Application range -- Cellulose nanofibers -- Composite fabrication -- Physio-chemical properties -- Polyethylene nanocomposites -- Thermo-mechanical analysis -- Uniform dispersions -- Viscoelastic properties -- Cellulose -- Aliphatic Compounds -- Cellulose -- Crystallization -- Fillers -- Plants -- Polyethylene -- Thermoplastics -- Viscoelasticity
Аннотация: The research on cellulose fiber-reinforced nanocomposites has increased by an unprecedented magnitude over the past few years due to its wide application range and low production cost. However, the incompatibility between cellulose and most thermoplastics has raised significant challenges in composite fabrication. This paper addresses the behavior of plasma-modified polyethylene (PE) reinforced with cellulose nanofibers extracted from isora plants (i.e., isora nanofibrils (INFs)). The crystallization kinetics of PE–INF composites were explained using the Avrami model. The effect of cellulose nanofillers on tuning the physiochemical properties of the nanocomposite was also explored in this work. The increase in mechanical properties was due to the uniform dispersion of fillers in the PE. The investigation on viscoelastic properties confirmed good filler–matrix interactions, facilitating the stress transfer. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Newman College, Thodupuzha, Kerala, 685585, India
Faculty of Applied Sciences, Universiti Teknologi MARA, Shah Alam, 40450, Malaysia
International and Inter University Centre for Nanoscience and Nanotechnology, Mahatma Gandhi University, Kottayam, Kerala, 686560, India
School of Energy Materials, Mahatma Gandhi University, Kottayam, Kerala, 686560, India
School of Chemical Sciences, Mahatma Gandhi University, Kottayam, Kerala, 686560, India
Institute of Biophysics of the Siberian Branch of the Russian Academy of Sciences, Siberian Federal University, 79 Svobodnyi Av., Krasnoyarsk, 660041, Russian Federation
Dipartimento di Ingegneria, Universita di Palermo, Viale delle Scienze, Palermo, 90128, Italy
Consorzio INSTM, Firenze, 50121, Italy
Institut Jean Lamour, UMR 7198, CNRS, Universite de Lorraine, Vandoeuvre-les-Nancy, F-54500, France
Facolta di Ingegneria, Universita degli Studi di Enna “Kore”, Cittadella Universitaria, Enna, 94100, Italy
Instituto de Alta Investigacion Universidad de Tarapaca, Casilla 7D, Arica, 1000000, Chile

Доп.точки доступа:
Jose, C.; Chan, C. H.; Winie, T.; Joseph, B.; Tharayil, A.; Maria, H. J.; Volova, T.; Mantia, F. P.L.; Rouxel, D.; Morreale, M.; Laroze, D.; Mathew, L.; Thomas, S.

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Constructing slow-release formulations of herbicide metribuzin using its co-extrusion with biodegradable polyester poly-ε-caprolactone / A. N. Boyandin, E. A. Kazantseva // J. Environ. Sci. Health Part B Pestic. Food Contamin. Agric. Wastes. - 2021, DOI 10.1080/03601234.2021.1911206 . - Article in press. - ISSN 0360-1234
Кл.слова (ненормированные):
extrusion -- herbicide -- long-term -- pesticide -- Polycaprolactone -- Biodegradable polymers -- Biodegradation -- Degradation -- Extrusion -- Melting -- Plastic coatings -- Polyesters -- Soils -- Weed control -- Biodegradable polyesters -- Degradation rate -- First-order models -- Long-term release -- Low cost methods -- Partial degradation -- Release kinetics -- Soil applications -- Herbicides
Аннотация: Different technologies to prepare long term pesticide forms include polymer coating, preparing composites and encapsulating pesticides in nanoparticles. A simple and low-cost method was proposed to obtain slow-release formulations by co-extrusion of a pesticide with a biodegradable polymer at a temperature above the melting points of both components. A herbicide metribuzin and low-melting polyester poly-?-caprolactone were chosen for this work. Formulations containing 10%, 20%, and 40% herbicide were prepared. During 7 days of their exposition in water, it was released from 81% to 96% of initially loaded metribuzin; the highest release was detected for 40%-loaded forms. Biodegradation of the constructs and pesticide release were further studied in the model soil. Degradation rates of the specimens increased with an increase in pesticide content, from 9% to 20% over 14 weeks for the 10%/20%-loaded and the 40%-loaded specimens, respectively. The release of metribuzin reached, respectively, 37–38% and 55%. The herbicide content in soil was lower due to its partial degradation in soil; it reached 23–25% and 33%, respectively, from initially loaded into the polymer matrix. Release kinetics of metribuzin in water as in soil best fitted the First-order model. The used approach is promising for obtaining long-term release formulations for soil applications. © 2021 Taylor & Francis Group, LLC.

Scopus
Держатели документа:
Institute of Biophysics of Siberian Branch of Russian Academy of Sciences, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Boyandin, A. N.; Kazantseva, E. A.

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Mechanisms of viscous media effects on elementary steps of bacterial bioluminescent reaction / A. E. Lisitsa, L. A. Sukovatyi, S. I. Bartsev [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 16. - Ст. 8827, DOI 10.3390/ijms22168827 . - ISSN 1661-6596
Кл.слова (ненормированные):
Bacterial luciferase -- Diffusion limitation -- Non-steady-state reaction kinetics -- Viscosity
Аннотация: Enzymes activity in a cell is determined by many factors, among which viscosity of the microenvironment plays a significant role. Various cosolvents can imitate intracellular conditions in vitro, allowing to reduce a combination of different regulatory effects. The aim of the study was to analyze the media viscosity effects on the rate constants of the separate stages of the bacterial biolumi-nescent reaction. Non-steady-state reaction kinetics in glycerol and sucrose solutions was measured by stopped-flow technique and analyzed with a mathematical model developed in accordance with the sequence of reaction stages. Molecular dynamics methods were applied to reveal the effects of cosolvents on luciferase structure. We observed both in glycerol and in sucrose media that the stages of luciferase binding with flavin and aldehyde, in contrast to oxygen, are diffusion-limited. More-over, unlike glycerol, sucrose solutions enhanced the rate of an electronically excited intermediate formation. The MD simulations showed that, in comparison with sucrose, glycerol molecules could penetrate the active-site gorge, but sucrose solutions caused a conformational change of functionally important ?Glu175 of luciferase. Therefore, both cosolvents induce diffusion limitation of substrates binding. However, in sucrose media, increasing enzyme catalytic constant neutralizes viscosity effects. The activating effect of sucrose can be attributed to its exclusion from the catalytic gorge of luciferase and promotion of the formation of the active site structure favorable for the catalysis. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Biophysics Department, Siberian Federal University, Svobodny 79, Krasnoyarsk, 660041, Russian Federation
The Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Lisitsa, A. E.; Sukovatyi, L. A.; Bartsev, S. I.; Deeva, A. A.; Kratasyuk, V. A.; Nemtseva, E. V.

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Thermal Inactivation of Butyrylcholinesterase in Starch and Gelatin Gels / V. I. Lonshakova-Mukina, E. N. Esimbekova, V. A. Kratasyuk // Catalysts. - 2021. - Vol. 11, Is. 4. - Ст. 492, DOI 10.3390/catal11040492. - Cited References:39. - The research was funded by the Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science, and the Russian Foundation for Basic Research [project No 20-44-242001]. . - ISSN 2073-4344

РУБ Chemistry, Physical

Кл.слова (ненормированные):
butyrylcholinesterase -- thermal inactivation -- enzyme stability -- kinetics -- starch -- gelatin
Аннотация: The present study demonstrates a simple approach to enhancing thermal stability of butyrylcholinesterase (BChE) by using natural polymers. Analysis of thermal inactivation of the tetrameric BChE in starch and gelatin gels at 50-64 degrees C showed that thermal inactivation followed second-order kinetics and involved two alternating processes of BChE inactivation, which occurred at different rates (fast and slow processes). The activation enthalpy Delta H-# and the activation entropy Delta S-# for BChE in starch and gelatin gels were evaluated. The values of Delta H-# for the fast and the slow thermal inactivation of BChE in starch gel were 61 +/- 3, and 22 +/- 2 kcal/mol, respectively, and the values of Delta S-# were 136 +/- 12 and -2.03 +/- 0.05 cal center dot K-1 center dot mol(-1), respectively. Likewise, the values of Delta H-# for BChE in gelatin gel were 58 +/- 6 and 109 +/- 11 kcal/mol, and the values of Delta S-# were 149 +/- 16 and 262 +/- 21 cal center dot K-1 center dot mol(-1), respectively. The values of the activation parameters obtained in this study suggest that starch gel produced a stronger stabilizing effect on BChE exposed to elevated temperatures over long periods compared with gelatin gel.

WOS
Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Biophys Dept, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Lonshakova-Mukina, Victoria I.; Esimbekova, Elena N.; Kratasyuk, Valentina A.; Government of Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-44-242001]

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10.

Thermomechanical Analysis of Isora Nanofibril Incorporated Polyethylene Nanocomposites / C. Jose, C. H. Chan, T. Winie [et al.] // Polymers. - 2021. - Vol. 13, Is. 2. - Ст. 299, DOI 10.3390/polym13020299. - Cited References:46. - This study (polymer synthesis and investigation) was financially supported by the project "Agro preparations of the new generation: a strategy of construction and realization" (Agreement No 074-02-2018-328) in accordance with Resolution No 220 of the Government of the Russian Federation on 9 April 2010, "On measures designed to attract leading scientists to the Russian institutions of higher learning". . - ISSN 2073-4360

РУБ Polymer Science

Кл.слова (ненормированные):
polymer-cellulose nanocomposites -- crystallization -- mechanical -- properties -- Avrami model
Аннотация: The research on cellulose fiber-reinforced nanocomposites has increased by an unprecedented magnitude over the past few years due to its wide application range and low production cost. However, the incompatibility between cellulose and most thermoplastics has raised significant challenges in composite fabrication. This paper addresses the behavior of plasma-modified polyethylene (PE) reinforced with cellulose nanofibers extracted from isora plants (i.e., isora nanofibrils (INFs)). The crystallization kinetics of PE-INF composites were explained using the Avrami model. The effect of cellulose nanofillers on tuning the physiochemical properties of the nanocomposite was also explored in this work. The increase in mechanical properties was due to the uniform dispersion of fillers in the PE. The investigation on viscoelastic properties confirmed good filler-matrix interactions, facilitating the stress transfer.

WOS
Держатели документа:
Newman Coll Educ, Thodupuzha 685585, Kerala, India.
Univ Teknol MARA, Fac Appl Sci, Shah Alam 40450, Malaysia.
Mahatma Gandhi Univ, Int & Inter Univ Ctr Nanosci & Nanotechnol, Kottayam 686560, Kerala, India.
Mahatma Gandhi Univ, Sch Energy Mat, Kottayam 686560, Kerala, India.
Mahatma Gandhi Univ, Sch Chem Sci, Kottayam 686560, Kerala, India.
Siberian Fed Univ, Russian Acad Sci, Siberian Branch, Inst Biophys, 79 Svobodnyi Av, Krasnoyarsk 660041, Russia.
Univ Palermo, Dipartimento Ingn, Viale Sci, I-90128 Palermo, Italy.
Consorzio INSTM, I-50121 Florence, Italy.
Univ Lorraine, CNRS, Inst Jean Lamour, UMR 7198, F-54500 Vandoeuvre Les Nancy, France.
Univ Studi Enna Kore, Facolta Ingn, Cittadella Univ, I-94100 Enna, Italy.
Univ Tarapaca, Inst Alta Invest, Casilla 7D, Arica 1000000, Chile.

Доп.точки доступа:
Jose, Cintil; Chan, Chin Han; Winie, Tan; Joseph, Blessy; Tharayil, Abhimanyu; Maria, Hanna J.; Volova, Tatiana; La Mantia, Francesco Paolo; Rouxel, Didier; Morreale, Marco; Laroze, David; Mathew, Lovely; Thomas, Sabu; La, Francesco Paolo; project "Agro preparations of the new generation: a strategy of construction and realization" [074-02-2018-328]; Government of the Russian Federation [220]

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11.

Constructing slow-release formulations of herbicide metribuzin using its co-extrusion with biodegradable polyester poly-epsilon-caprolactone / A. N. Boyandin, E. A. Kazantseva // J. Environ. Sci. Health Part B-Pestic. Contam. Agric. Wastes. - 2021, DOI 10.1080/03601234.2021.1911206. - Cited References:43. - This study was financially supported by Project "Agropreparations of the new generation: a strategy of construction and realization" (Agreement No 074-02-2018-328) in accordance with Resolution No 220 of the Government of the Russian Federation of April 9, 2010, "On measures designed to attract leading scientists to the Russian institutions of higher learning". . - Article in press. - ISSN 0360-1234. - ISSN 1532-4109

РУБ Environmental Sciences + Public, Environmental & Occupational Health

Кл.слова (ненормированные):
Polycaprolactone -- herbicide -- pesticide -- long-term -- extrusion
Аннотация: Different technologies to prepare long term pesticide forms include polymer coating, preparing composites and encapsulating pesticides in nanoparticles. A simple and low-cost method was proposed to obtain slow-release formulations by co-extrusion of a pesticide with a biodegradable polymer at a temperature above the melting points of both components. A herbicide metribuzin and low-melting polyester poly-epsilon-caprolactone were chosen for this work. Formulations containing 10%, 20%, and 40% herbicide were prepared. During 7 days of their exposition in water, it was released from 81% to 96% of initially loaded metribuzin; the highest release was detected for 40%-loaded forms. Biodegradation of the constructs and pesticide release were further studied in the model soil. Degradation rates of the specimens increased with an increase in pesticide content, from 9% to 20% over 14 weeks for the 10%/20%-loaded and the 40%-loaded specimens, respectively. The release of metribuzin reached, respectively, 37-38% and 55%. The herbicide content in soil was lower due to its partial degradation in soil; it reached 23-25% and 33%, respectively, from initially loaded into the polymer matrix. Release kinetics of metribuzin in water as in soil best fitted the First-order model. The used approach is promising for obtaining long-term release formulations for soil applications.

WOS
Держатели документа:
Russian Acad Sci, Krasnoyarsk Sci Ctr SB RAS, Fed Res Ctr, Inst Biophys,Siberian Branch, 50-50 Akademgorodok, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Boyandin, Anatoly N.; Kazantseva, Eugenia A.; Boyandin, Anatoly; Project "Agropreparations of the new generation: a strategy of construction and realization" [074-02-2018-328]; Government of the Russian Federation [220]

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12.

Coelenterazine-dependent luciferases as a powerful analytical tool for research and biomedical applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465. - P1-31, DOI 10.3390/ijms21207465 . - ISSN 1661-6596
Кл.слова (ненормированные):
Analytical systems -- Bioluminescence -- Ca2+-regulated photoprotein -- Coelenterazine -- Luciferase
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate—coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization—Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme–substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
School of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Krasitskaya, V. V.; Bashmakova, E. E.; Frank, L. A.

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13.

Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents / E. V. Eremeeva, T. Y. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446, DOI 10.3390/ijms21155446. - Cited References:50. - The reported study was funded by RFBR and NSFC according to the research project No. 20-54-53011 (E.V.E. and N.P.M.), Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (E.S.V.), the National Natural Science Foundation of China (No. 81874308), and the Shandong Natural Science Foundation (No. ZR2018ZC0233) (M.L.). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Кл.слова (ненормированные):
photoprotein -- obelin -- aequorin -- coelenterazine -- analogues
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues.

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Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Shandong Univ, Sch Pharmaceut Sci, Dept Med Chem, Key Lab Chem Biol MOE, Jinan 250012, Peoples R China.
Shandong Univ, Helmholtz Inst Biotechnol, State Key Lab Microbial Technol, Qingdao 266237, Peoples R China.

Доп.точки доступа:
Eremeeva, Elena, V; Jiang, Tianyu; Malikova, Natalia P.; Li, Minyong; Vysotski, Eugene S.; RFBRRussian Foundation for Basic Research (RFBR); NSFCNational Natural Science Foundation of China (NSFC) [20-54-53011]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [81874308]; Shandong Natural Science FoundationNatural Science Foundation of Shandong Province [ZR2018ZC0233]; Government of Krasnoyarsk Territory

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14.

Bioluminescent properties of semi-synthetic obelin and aequorin activated by coelenterazine analogues with modifications of C-2, C-6, and C-8 substituents / E. V. Eremeeva, T. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446. - P1-21, DOI 10.3390/ijms21155446 . - ISSN 1661-6596
Кл.слова (ненормированные):
Aequorin -- Analogues -- Coelenterazine -- Obelin -- Photoprotein
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Key Laboratory of Chemical Biology (MOE), Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan, Shandong 250012, China
State Key Laboratory of Microbial Technology, Shandong University–Helmholtz Institute of Biotechnology, Shandong University, Qingdao, Shandong 266237, China

Доп.точки доступа:
Eremeeva, E. V.; Jiang, T.; Malikova, N. P.; Li, M.; Vysotski, E. S.

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15.

The Effect of Osmolytes on the Bioluminescent Reaction of Bacteria: Structural and Dynamic Properties / L. A. Sukovatyi, A. E. Lisitsa, V. A. Kratasyuk, E. V. Nemtseva // Biophysics. - 2020. - Vol. 65, Is. 6. - P966-971, DOI 10.1134/S0006350920060202 . - ISSN 0006-3509
Кл.слова (ненормированные):
bacterial luciferase -- bioluminescence -- luminous bacteria -- molecular dynamic -- osmolyte -- protein structure and dynamics
Аннотация: The effects of viscous media with glycerol and sucrose (10–40%) on the kinetics of the bacterial bioluminescent reaction have been investigated by stopped-flow technique. Increment of quantum yield in media with 10% of both osmolytes was shown. Higher concentrations of glycerol, up to 30–40%, were found to reduce the efficiency of the reaction, while this effect was not observed in the media with sucrose. The molecular dynamics simulation was used to study the structure of bacterial luciferase surrounded by either water molecules solely or by mixture of water with various numbers of glycerol/sucrose molecules. It was found that both cosolvents at studied concentrations did not cause a significant change in conformation of bacterial luciferase. The calculated root-mean-square fluctuation for C?-atoms of bacterial luciferase ?-subunit indicated that the higher flexibility of the enzyme mobile loop could be responsible for increment of quantum yield in the presence of 10% of both osmolytes. The active site of bacterial luciferase was found to be accessible for glycerol molecules while sucrose did not enter catalytic gorge. Moreover, at 30 and 40% concentration the glycerol molecules were found to locate in the active site of bacterial luciferase throughout the whole simulation time. © 2020, Pleiades Publishing, Inc.

Scopus
Держатели документа:
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Sukovatyi, L. A.; Lisitsa, A. E.; Kratasyuk, V. A.; Nemtseva, E. V.

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16.

Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465, DOI 10.3390/ijms21207465. - Cited References:251. - The work was supported by the Russian State funded budget project of IBP SB RAS No. AAAA-A19-119031890015-0. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
PROTEIN-PROTEIN INTERACTIONS
CA2+-REGULATED PHOTOPROTEIN OBELIN
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- Ca2+-regulated -- photoprotein -- analytical systems
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate-coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization-Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme-substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Bashmakova, Eugenia E.; Frank, Ludmila A.; Russian State funded budget project of IBP SB RAS [AAAA-A19-119031890015-0]

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17.

18.

An elementary multistage discrete model of soil organic matter transformations with a continuous scale of stability / S. I. Bartsev, A. A. Pochekutov // Ecol. Model. - 2019. - Vol. 393. - P61-65, DOI 10.1016/j.ecolmodel.2018.12.012 . - ISSN 0304-3800
Кл.слова (ненормированные):
Kinetics of soil organic matter transformations -- Model of soil organic matter transformations -- Soil organic matter -- Biogeochemistry -- Biological materials -- Decay (organic) -- Organic compounds -- Soils -- Continuous scale -- Discrete modeling -- Elementary model -- Law of mass action -- Multistage process -- Realistic model -- Soil organic matters -- Transformation process -- Mathematical transformations -- biotransformation -- chemical alteration -- decomposition -- numerical model -- reaction kinetics -- soil organic matter
Аннотация: The proposed elementary mathematical model of formation and decomposition of soil organic matter (SOM) is based on using equations of chemical kinetics to describe the multistage process of SOM transformation. The model both describes each step of transformation in accordance with the law of mass action and postulates the trend of increasing stability of the matter towards further transformation, which is common for all steps. Analysis of the model demonstrates that it is extremely difficult to construct a realistic model of SOM dynamics by assembling elementary models of the type presented in this study into the full description of SOM transformation processes. © 2018 Elsevier B.V.

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Institute of Fundamental Biology and Biotechnology of Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Bartsev, S. I.; Pochekutov, A. A.

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19.

Exploring Bioluminescence Function of the Ca2+-regulated Photoproteins with Site-directed Mutagenesis / E. V. Eremeeva, E. S. Vysotski // Photochem. Photobiol. - 2019. - Vol. 95, Is. 1. - P8-23, DOI 10.1111/php.12945. - Cited References:88. - This work was supported by grant 17-04-00764 of Russian Foundation for Basic Research and the state budgetallocated to the fundamental research at the Russian Academy of Sciences (project 0356-2017-0017). . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CALCIUM-BINDING PHOTOPROTEIN
GREEN-FLUORESCENT PROTEIN
JELLYFISH
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- aequorin -- obelin -- clytin -- mitrocomin -- EF-hand protein
Аннотация: Site-directed mutagenesis is a powerful tool to investigate the structure-function relationship of proteins and a function of certain amino acid residues in catalytic conversion of substrates during enzymatic reactions. Hence, it is not surprising that this approach was repeatedly applied to elucidate the role of certain amino acid residues in various aspects of photoprotein bioluminescence, mostly for aequorin and obelin, and to design mutant photoproteins with altered properties (modified calcium affinity, faster or slower bioluminescence kinetics, different emission color) which would either allow the development of novel bioluminescent assays or improvement of characteristics of the already existing ones. This information, however, is scattered over different articles. In this review, we systematize the findings that were made using site-directed mutagenesis studies regarding the impact of various amino acid residues on bioluminescence of hydromedusan Ca2+-regulated photoproteins. All key residues that have been identified are pinpointed, and their influence on different aspects of photoprotein functioning such as active photoprotein complex formation, bioluminescence reaction, calcium response and light emitter formation is discussed.

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Держатели документа:
RAS, SB, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr,Photobiol Lab, Krasnoyarsk, Russia.

Доп.точки доступа:
Eremeeva, Elena V.; Vysotski, Eugene S.; Russian Foundation for Basic Research [17-04-00764]; Russian Academy of Sciences [0356-2017-0017]

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20.

Role of Hsp90 and ATP in modulating apyrase activity and firefly luciferase kinetics / M. A. Kirillova [et al.] // Int. J. Biol. Macromol. - 2019. - Vol. 131. - P691-696, DOI 10.1016/j.ijbiomac.2019.03.110 . - ISSN 0141-8130
Кл.слова (ненормированные):
Bioluminescence -- Heat shock protein 90 -- High-throughput screening -- adenosine triphosphate -- apyrase -- bovine serum albumin -- firefly luciferase -- heat shock protein 90 -- stabilizing agent -- Article -- bioluminescence -- clinical study -- conformation -- controlled study -- denaturation -- enzyme activity -- enzyme kinetics -- high throughput screening -- incubation time -- nonhuman -- protein protein interaction -- protein refolding -- temperature -- thermal denaturation -- time
Аннотация: The present manuscript describes a novel bioassay consisting of apyrase and heat shock protein 90 (Hsp90) without additional co-chaperone supplementation; intended for high-throughput screening of anti-cancer drugs and prognosis of stress. In this regard, Hsp90 and adenosine 5?-triphosphate (ATP) mediated firefly luciferase (FLuc) kinetics was investigated using apyrase and FLuc as client proteins. Bioluminescent assay containing Hsp90, ATP, and apyrase led to complete loss of luminescence at 50 °C which indicates the protective role of Hsp90 against thermal denaturation. Similarly, the assay sample comprising Hsp90, ATP, and FLuc showed 2 fold increments in luminescence than their counterparts. Introduction of bovine serum albumin (BSA) to the pre-incubated assay mixture led to an initial rise in the luminescence (28%) in comparison to the sample containing Hsp90, ATP and FLuc. Therefore, FLuc based HTS assays are not suitable for clinical samples which may contain stabilizing agents. However, thermally denatured FLuc and apyrase could not regain their active conformation even when Hsp90 and ATP were introduced in the assay system. This observation justifies the role of Hsp90 to be protective rather than a reparation agent when acts without co-chaperones. © 2019

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Держатели документа:
Laboratory of Bioluminescent Biotechnologies, Department of Biophysics, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, 79 Svobodny Prospect, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Kirillova, M. A.; Ranjan, R.; Esimbekova, E. N.; Kratasyuk, V. A.

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