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  1. Artikel ; Online: Preparation of Catalase Cross-Linked Aggregates Based on Vaterite Matrix

    Tagirova, M. A. / Eremeev, N. L. / Balabushevich, N. G. / Volodkin, D. V. / Klyachko, N. L.

    Appl Biochem Microbiol. 2022 Dec., v. 58, no. 8 p.923-931

    2022  

    Abstract: A new technique has been developed for the synthesis of cross-linked catalase aggregates by treatment of the enzyme incorporated into the pores of vaterite microspheres with glutaraldehyde and subsequent dissolving of the inorganic matrix. The resulting ... ...

    Abstract A new technique has been developed for the synthesis of cross-linked catalase aggregates by treatment of the enzyme incorporated into the pores of vaterite microspheres with glutaraldehyde and subsequent dissolving of the inorganic matrix. The resulting aggregates have a spherical shape, a narrow particle size distribution, and a high specific activity. The number and enzyme activity of the cross-linked aggregates strongly depends on the rate of the matrix dissolution: mild conditions of dissolution made it possible to increase the number of formed protein particles, whose residual catalase specific activity was only 2 times less than that of the native enzyme. The storage stability of the cross-linked aggregates is comparable to that of the native enzyme of the same concentration.
    Schlagwörter catalase ; crosslinking ; enzyme activity ; glutaraldehyde ; microparticles ; particle size distribution ; storage quality ; vaterite
    Sprache Englisch
    Erscheinungsverlauf 2022-12
    Umfang p. 923-931.
    Erscheinungsort Pleiades Publishing
    Dokumenttyp Artikel ; Online
    ZDB-ID 412550-2
    ISSN 1608-3024 ; 0003-6838
    ISSN (online) 1608-3024
    ISSN 0003-6838
    DOI 10.1134/S0003683822080075
    Datenquelle NAL Katalog (AGRICOLA)

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  2. Artikel ; Online: Analysis of Cytokines and ATP in Plucked Hair Follicles.

    Mikhalchik, E V / Morozova, O V / Tsimbalenko, T V / Kharaeva, Z F / Balabushevich, N G / Lipatova, V A / Gadzhigoroeva, A G

    Bulletin of experimental biology and medicine

    2021  Band 170, Heft 3, Seite(n) 299–302

    Abstract: The concentrations of ATP, IL-6, and IL-10 were measured in extracts of plucked hair follicles from healthy volunteers (normal values) and patients with androgenetic alopecia and then, ATP, IL-6, and IL-10 content was calculated for each follicle. The ... ...

    Abstract The concentrations of ATP, IL-6, and IL-10 were measured in extracts of plucked hair follicles from healthy volunteers (normal values) and patients with androgenetic alopecia and then, ATP, IL-6, and IL-10 content was calculated for each follicle. The resulting values were directly proportional to hair follicle length, except for IL-6. The concentration of extracted ATP correlated with lactate dehydrogenase activity indicating cell damage. In patients with androgenetic alopecia, IL-10 content exceeded the normal values in follicles with a length <1 mm and ATP content surpassed the normal in follicles >2 mm long. The content of IL-6 and IL-10 measured by ELISA was comparable with results of mRNA expression assayed by RT-PCR, which attested to moderate level of gene expression. The content of ATP and IL- 10, but not IL-6 depended on the length of plucked hair follicle and on pathogenetic factors affecting hair growth.
    Mesh-Begriff(e) Adenosine Triphosphate/analysis ; Animals ; Cytokines/analysis ; Enzyme-Linked Immunosorbent Assay ; Female ; Hair Follicle/chemistry ; Interleukin-10/analysis ; Interleukin-6/analysis ; Male ; Rats ; Rats, Wistar
    Chemische Substanzen Cytokines ; Interleukin-6 ; Interleukin-10 (130068-27-8) ; Adenosine Triphosphate (8L70Q75FXE)
    Sprache Englisch
    Erscheinungsdatum 2021-01-16
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 390407-6
    ISSN 1573-8221 ; 0007-4888 ; 0365-9615
    ISSN (online) 1573-8221
    ISSN 0007-4888 ; 0365-9615
    DOI 10.1007/s10517-021-05055-0
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: The mechanism of catalase loading into porous vaterite CaCO

    Vikulina, A S / Feoktistova, N A / Balabushevich, N G / Skirtach, A G / Volodkin, D

    Physical chemistry chemical physics : PCCP

    2018  Band 20, Heft 13, Seite(n) 8822–8831

    Abstract: Porous vaterite CaCO3 crystals are nowadays extensively used as high-capacity bio-friendly sacrificial templates for the fabrication of such protein-containing nano- and micro-particles as capsules and beads. The first step in the protein encapsulation ... ...

    Abstract Porous vaterite CaCO3 crystals are nowadays extensively used as high-capacity bio-friendly sacrificial templates for the fabrication of such protein-containing nano- and micro-particles as capsules and beads. The first step in the protein encapsulation is performed through loading of the protein molecules into the crystals. Co-synthesis is one of the most useful and simple methods proven to effectively load crystals with proteins; however, the loading mechanism is still unknown. To understand the mechanism, in this study, we focus on the loading of a model protein catalase into the crystals by means of adsorption into pre-formed crystals (ADS) and co-synthesis (COS). Analysis of the physico-chemical characteristics of the protein in solution and during the loading and simulation of the protein packing into the crystals are performed. COS provides more effective loading than ADS giving protein contents in the crystals of 20.3 and 3.5 w/w%, respectively. Extremely high loading for COS providing a local protein concentration of about 550 mg mL-1 is explained by intermolecular protein interactions, i.e. formation of protein aggregates induced by CaCl2 during the co-synthesis. This is supported by a lower equilibrium constant obtained for COS (5 × 105 M-1) than for ADS (23 × 105 M-1), indicating a higher affinity of single protein molecules rather than aggregates to the crystal surface. Fitting the adsorption isotherms by classical adsorption models has shown that the Langmuir and BET models describe the adsorption phenomenon better than the Freundlich model, proving the aggregation in solution followed by adsorption of the aggregates into the crystals. We believe that this study will be useful for protein encapsulation through CaCO3 crystals using the COS method.
    Mesh-Begriff(e) Calcium Carbonate/chemistry ; Catalase/chemistry ; Catalase/metabolism
    Chemische Substanzen Catalase (EC 1.11.1.6) ; Calcium Carbonate (H0G9379FGK)
    Sprache Englisch
    Erscheinungsdatum 2018-03-28
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 1476244-4
    ISSN 1463-9084 ; 1463-9076
    ISSN (online) 1463-9084
    ISSN 1463-9076
    DOI 10.1039/c7cp07836f
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Inter-protein interactions govern protein loading into porous vaterite CaCO3 crystals

    Feoktistova, N.A. / Balabushevich, N.G. / Skirtach, A.G. / Volodkin, D. / Vikulina, A.S.

    2020  

    Abstract: S.9713-9722 ... The fast development of protein therapeutics has resulted in a high demand for advanced delivery carriers that can effectively host therapeutic proteins, preserve their bioactivity and release them on demand. Accordingly, vaterite CaCO3 ... ...

    Abstract S.9713-9722

    The fast development of protein therapeutics has resulted in a high demand for advanced delivery carriers that can effectively host therapeutic proteins, preserve their bioactivity and release them on demand. Accordingly, vaterite CaCO3 crystals have attracted special attention as sacrificial templates for protein encapsulation in micro- and nanoparticles (capsules and beads, respectively) under mild biofriendly conditions. This study aimed to better understand the mechanism of protein loading into crystals as a primary step for protein encapsulation. The loading of three therapeutic proteins (250 kDa catalase, 5.8 kDa insulin, and 6.5 kDa aprotinin) was investigated for crystals with different porosities. However, unexpectedly, the protein loading capacity was not consistent with the protein molecular weight. It solely depends on the inter-protein interactions in the bulk solution in the presence of crystals and that inside the crystals. The smallest protein aprotinin aggregates in the bulk (its aggregate size is about 100 nm), which prohibits its loading into the crystals. Insulin forms hexamers in the bulk, which can diffuse into the crystal pores but tend to aggregate inside the pores, suppressing protein diffusion inward. Catalase, the largest protein tested, does not form any aggregates in the bulk and diffuses freely into the crystals; however, its diffusion into small pores is sterically restricted. These findings are essential for the encapsulation of protein therapeutics by means of templating based on CaCO3 crystals and for the engineering of protein-containing microparticles having desired architectures.

    22

    Nr.17
    Schlagwörter 610 ; 541 ; 620
    Thema/Rubrik (Code) 612
    Sprache Englisch
    Erscheinungsland de
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  5. Artikel ; Online: Bioactivity of catalase loaded into vaterite CaCO3 crystals via adsorption and co-synthesis

    Feoktistova, N.A. / Vikulina, A.S. / Balabushevich, N.G. / Skirtach, A.G. / Volodkin, D.

    2020  

    Abstract: Art. 108223, 10 S. ... Protein therapy gained a reputation of the most direct and safe approach for treating various diseases, yet biodegradation and loss of bioactivity of fragile therapeutic proteins limit their wide medical use. Recently, a new hard ... ...

    Abstract Art. 108223, 10 S.

    Protein therapy gained a reputation of the most direct and safe approach for treating various diseases, yet biodegradation and loss of bioactivity of fragile therapeutic proteins limit their wide medical use. Recently, a new hard templating technology using decomposable mesoporous vaterite CaCO3 crystals became extremely popular strategy for formulation of protein nano(micro)-vectors. This study deciphers how protein bioactivity depends on protein loading/release for this technology utilizing catalase as a promising antioxidant therapeutic agent. Catalase has been loaded into CaCO3 using two approaches: i) passive - via adsorption (ADS) into pre-formed crystals and ii) active - via co-synthesis (COS) in the pH range 8-10. Crystal morphology, protein secondary structure and enzymatic bioactivity, and protein retention upon washing are assessed. The activity reduction (∼70% for COS and ∼20% for ADS) is caused by both protein exposure to an alkaline medium and protein aggregation induced by Ca2+. The aggregation significantly governs protein release kinetics. Catalase loading into the crystals is pH-independent and van der Waals interactions dominate over the electrostatics, while catalase activity strongly depends on pH. This study implicates the prime role of loading/release mechanism in the preservation of protein bioactivity and guide for the control over the retention of protein bioactivity.

    185
    Schlagwörter 610 ; 620
    Thema/Rubrik (Code) 572
    Sprache Englisch
    Erscheinungsland de
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  6. Artikel ; Online: The mechanism of catalase loading into porous vaterite CaCO3 crystals by co-synthesis

    Vikulina, A.S. / Feoktistova, N.A. / Balabushevich, N.G. / Skirtach, A.G. / Volodkin, D.

    2018  

    Abstract: S.8822-8831 ... Porous vaterite CaCO3 crystals are nowadays extensively used as high-capacity bio-friendly sacrificial templates for the fabrication of such protein-containing nano- and micro-particles as capsules and beads. The first step in the protein ... ...

    Abstract S.8822-8831

    Porous vaterite CaCO3 crystals are nowadays extensively used as high-capacity bio-friendly sacrificial templates for the fabrication of such protein-containing nano- and micro-particles as capsules and beads. The first step in the protein encapsulation is performed through loading of the protein molecules into the crystals. Co-synthesis is one of the most useful and simple methods proven to effectively load crystals with proteins; however, the loading mechanism is still unknown. To understand the mechanism, in this study, we focus on the loading of a model protein catalase into the crystals by means of adsorption into pre-formed crystals (ADS) and co-synthesis (COS). Analysis of the physico-chemical characteristics of the protein in solution and during the loading and simulation of the protein packing into the crystals are performed. COS provides more effective loading than ADS giving protein contents in the crystals of 20.3 and 3.5 w/w%, respectively. Extremely high loading for COS providing a local protein concentration of about 550 mg mL−1 is explained by intermolecular protein interactions, i.e. formation of protein aggregates induced by CaCl2 during the co-synthesis. This is supported by a lower equilibrium constant obtained for COS (5 × 105 M−1) than for ADS (23 × 105 M−1), indicating a higher affinity of single protein molecules rather than aggregates to the crystal surface. Fitting the adsorption isotherms by classical adsorption models has shown that the Langmuir and BET models describe the adsorption phenomenon better than the Freundlich model, proving the aggregation in solution followed by adsorption of the aggregates into the crystals. We believe that this study will be useful for protein encapsulation through CaCO3 crystals using the COS method.

    20

    Nr.13
    Schlagwörter 610 ; 620
    Thema/Rubrik (Code) 612
    Sprache Englisch
    Erscheinungsland de
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  7. Artikel ; Online: Protein loading into porous CaCO3 microspheres: adsorption equilibrium and bioactivity retention.

    Balabushevich, N G / Lopez de Guerenu, A V / Feoktistova, N A / Volodkin, D

    Physical chemistry chemical physics : PCCP

    2015  Band 17, Heft 4, Seite(n) 2523–2530

    Abstract: Formulation of proteins into particulate form is a principal strategy to achieve controlled and targeted delivery, as well as to protect fragile protein molecules. Control over size, mechanical properties, and surface area (porosity) of particulate ... ...

    Abstract Formulation of proteins into particulate form is a principal strategy to achieve controlled and targeted delivery, as well as to protect fragile protein molecules. Control over size, mechanical properties, and surface area (porosity) of particulate proteins has been successfully achieved by hard templating under mild conditions using porous CaCO3 microspheres. A crucial step in this approach, which determines protein content, is the loading of proteins into the CaCO3 microspheres. In this study, the adsorption of different proteins into the microspheres has been investigated. Proteins differing in characteristics such as molecular weight and charge have been employed: catalase (Cat), insulin (Ins), aprotinin (Apr), and protamine (Pro). Thermodynamics of adsorption equilibria have been studied, together with quantitative and qualitative analysis of protein loading and distribution in the microspheres. Protein interaction with the CaCO3 microspheres is not limited by the diffusion of protein molecules (protein dimensions are significantly smaller than microsphere pores) but is determined by the protein affinity for the microsphere surface. Cat and Ins bind much more strongly to the microspheres than Apr and Pro, which can be explained by electrostatic attractive forces. Protein binding/release and protein biological activity have been investigated as a function of pH. It is shown that pH variation during the adsorption process plays a principal role and defines not only the amount of protein adsorbed/released but also protein biological activity. Protein adsorption and microsphere elimination (by EDTA) do not affect protein bioactivity. In addition to applications for protein particle/capsule formulations, the findings of this study might help in understanding protein interactions with carbonate minerals such as calcium carbonate, which is used as a natural material for multiple applications.
    Mesh-Begriff(e) Adsorption ; Animals ; Calcium Carbonate/chemistry ; Cattle ; Microspheres ; Porosity ; Proteins/chemistry
    Chemische Substanzen Proteins ; Calcium Carbonate (H0G9379FGK)
    Sprache Englisch
    Erscheinungsdatum 2015-01-28
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1476244-4
    ISSN 1463-9084 ; 1463-9076
    ISSN (online) 1463-9084
    ISSN 1463-9076
    DOI 10.1039/c4cp04567j
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel: Fabrication and characterization of polyelectrolyte microparticles with protein.

    Balabushevich, N G / Larionova, N I

    Biochemistry. Biokhimiia

    2004  Band 69, Heft 7, Seite(n) 757–762

    Abstract: The incorporation of proteins into microparticles fabricated by layer-by-layer adsorption of oppositely charged polyelectrolytes (dextran sulfate and protamine) on protein microaggregates was studied. Microaggregates with insulin were prepared by two ... ...

    Abstract The incorporation of proteins into microparticles fabricated by layer-by-layer adsorption of oppositely charged polyelectrolytes (dextran sulfate and protamine) on protein microaggregates was studied. Microaggregates with insulin were prepared by two different techniques: 1) formation of insoluble polyelectrolyte complex consisting of insulin and dextran sulfate (aggregate size of 7-20 micro m), or 2) salting out of insulin from solution by sodium chloride (aggregate size of 5-13 micro m). Microparticles varying in the number of cycles (from 1 to 8) of polyelectrolyte adsorption on protein aggregates were examined and compared. Morphology of the microparticles was studied by scanning electron and optical microscopy. It was shown that polyelectrolyte microparticles retained the shape and dimensions of the initial protein aggregates used as a template. Ultrasonication of microparticles obtained using salted out protein aggregates resulted in the formation of stable nanoparticles (100-200 nm). Regulation of protein release from the microparticles of both types by varying the number of polyelectrolyte adsorption cycles and pH of the medium was demonstrated. Insulin not bound to polyelectrolytes was released from the microparticles at pH values between 6 and 8, which corresponds to the pH of the human small intestine and ileum.
    Mesh-Begriff(e) Adsorption ; Dextran Sulfate/chemistry ; Electrolytes/chemistry ; Insulin/chemistry ; Particle Size ; Polymers/chemistry ; Protamines/chemistry ; Proteins/chemistry
    Chemische Substanzen Electrolytes ; Insulin ; Polymers ; Protamines ; Proteins ; Dextran Sulfate (9042-14-2)
    Sprache Englisch
    Erscheinungsdatum 2004-07-21
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1109-5
    ISSN 1608-3040 ; 0006-2979 ; 0320-9717
    ISSN (online) 1608-3040
    ISSN 0006-2979 ; 0320-9717
    DOI 10.1023/b:biry.0000040200.61663.01
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  9. Artikel ; Online: Binding of Mucin by E. coli from Human Gut.

    Vakhrusheva, T V / Baikova, Yu P / Balabushevich, N G / Gusev, S A / Lomakina, G Yu / Sholina, E A / Moshkovskaya, M A / Shcherbakov, P L / Pobeguts, O V / Mikhal'chik, E V

    Bulletin of experimental biology and medicine

    2018  Band 165, Heft 2, Seite(n) 235–238

    Abstract: Cells of E. coli isolates from the gut of healthy volunteers (N=5) and patients with Crohn's disease (N=5) and laboratory E. coli strain DH5α bound mucin in vitro in similar amounts ranging from 0.02 to 0.12 mg/mg of bacterial dry weight. Binding was ... ...

    Abstract Cells of E. coli isolates from the gut of healthy volunteers (N=5) and patients with Crohn's disease (N=5) and laboratory E. coli strain DH5α bound mucin in vitro in similar amounts ranging from 0.02 to 0.12 mg/mg of bacterial dry weight. Binding was evaluated by the decrease in optical absorption of mucin solution at 214 nm after incubation with bacteria. Detailed analysis of mucin binding by one of isolates showed that during incubation of 0.09 mg/ml bacteria in 0.15 M NaCl containing 0.1 mg/ml mucin at 25
    Mesh-Begriff(e) Bacterial Adhesion ; Crohn Disease/metabolism ; Crohn Disease/microbiology ; Crohn Disease/pathology ; Escherichia coli/isolation & purification ; Escherichia coli/metabolism ; Feces/microbiology ; Gastrointestinal Microbiome ; Healthy Volunteers ; Humans ; Intestines/microbiology ; Intestines/pathology ; Mucins/metabolism ; Protein Binding
    Chemische Substanzen Mucins
    Sprache Englisch
    Erscheinungsdatum 2018-06-19
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 390407-6
    ISSN 1573-8221 ; 0007-4888 ; 0365-9615
    ISSN (online) 1573-8221
    ISSN 0007-4888 ; 0365-9615
    DOI 10.1007/s10517-018-4137-3
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Protein loading into porous CaCO3 microspheres

    Balabushevich, N.G. / Lopez de Guerenu, A.V. / Feoktistovab, Natalia A. / Volodkin, D

    Adsorption equilibrium and bioactivity retention

    2015  

    Abstract: S.2523-2530 ... Formulation of proteins into particulate form is a principal strategy to achieve controlled and targeted delivery, as well as to protect fragile protein molecules. Control over size, mechanical properties, and surface area (porosity) of ... ...

    Abstract S.2523-2530

    Formulation of proteins into particulate form is a principal strategy to achieve controlled and targeted delivery, as well as to protect fragile protein molecules. Control over size, mechanical properties, and surface area (porosity) of particulate proteins has been successfully achieved by hard templating under mild conditions using porous CaCO3 microspheres. A crucial step in this approach, which determines protein content, is the loading of proteins into the CaCO3 microspheres. In this study, the adsorption of different proteins into the microspheres has been investigated. Proteins differing in characteristics such as molecular weight and charge have been employed: catalase (Cat), insulin (Ins), aprotinin (Apr), and protamine (Pro). Thermodynamics of adsorption equilibria have been studied, together with quantitative and qualitative analysis of protein loading and distribution in the microspheres. Protein interaction with the CaCO3 microspheres is not limited by the diffusion of protein molecules (protein dimensions are significantly smaller than microsphere pores) but is determined by the protein affinity for the microsphere surface. Cat and Ins bind much more strongly to the microspheres than Apr and Pro, which can be explained by electrostatic attractive forces. Protein binding/release and protein biological activity have been investigated as a function of pH. It is shown that pH variation during the adsorption process plays a principal role and defines not only the amount of protein adsorbed/released but also protein biological activity. Protein adsorption and microsphere elimination (by EDTA) do not affect protein bioactivity. In addition to applications for protein particle/capsule formulations, the findings of this study might help in understanding protein interactions with carbonate minerals such as calcium carbonate, which is used as a natural material for multiple applications.

    17

    Nr.4
    Schlagwörter 610 ; 541 ; 620
    Thema/Rubrik (Code) 612
    Sprache Englisch
    Erscheinungsland de
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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