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Article ; 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.
Keywords	catalase ; crosslinking ; enzyme activity ; glutaraldehyde ; microparticles ; particle size distribution ; storage quality ; vaterite
Language	English
Dates of publication	2022-12
Size	p. 923-931.
Publishing place	Pleiades Publishing
Document type	Article ; Online
ZDB-ID	412550-2
ISSN	1608-3024 ; 0003-6838
ISSN (online)	1608-3024
ISSN	0003-6838
DOI	10.1134/S0003683822080075
Database	NAL-Catalogue (AGRICOLA)

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Article ; 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 Volume 170, Issue 3, Page(s) 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 term(s)	Adenosine Triphosphate/analysis ; Animals ; Cytokines/analysis ; Enzyme-Linked Immunosorbent Assay ; Female ; Hair Follicle/chemistry ; Interleukin-10/analysis ; Interleukin-6/analysis ; Male ; Rats ; Rats, Wistar
Chemical Substances	Cytokines ; Interleukin-6 ; Interleukin-10 (130068-27-8) ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2021-01-16
Publishing country	United States
Document type	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
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Article ; 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
Keywords	610 ; 620
Subject code	572
Language	English
Publishing country	de
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; 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
Keywords	610 ; 541 ; 620
Subject code	612
Language	English
Publishing country	de
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; 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 Volume 20, Issue 13, Page(s) 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 term(s)	Calcium Carbonate/chemistry ; Catalase/chemistry ; Catalase/metabolism
Chemical Substances	Catalase (EC 1.11.1.6) ; Calcium Carbonate (H0G9379FGK)
Language	English
Publishing date	2018-03-28
Publishing country	England
Document type	Journal Article
ZDB-ID	1476244-4
ISSN	1463-9084 ; 1463-9076
ISSN (online)	1463-9084
ISSN	1463-9076
DOI	10.1039/c7cp07836f
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Article ; 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
Keywords	610 ; 620
Subject code	612
Language	English
Publishing country	de
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; 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 Volume 17, Issue 4, Page(s) 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 term(s)	Adsorption ; Animals ; Calcium Carbonate/chemistry ; Cattle ; Microspheres ; Porosity ; Proteins/chemistry
Chemical Substances	Proteins ; Calcium Carbonate (H0G9379FGK)
Language	English
Publishing date	2015-01-28
Publishing country	England
Document type	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
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Fabrication and characterization of polyelectrolyte microparticles with protein.

Balabushevich, N G / Larionova, N I

Biochemistry. Biokhimiia

2004 Volume 69, Issue 7, Page(s) 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 term(s)	Adsorption ; Dextran Sulfate/chemistry ; Electrolytes/chemistry ; Insulin/chemistry ; Particle Size ; Polymers/chemistry ; Protamines/chemistry ; Proteins/chemistry
Chemical Substances	Electrolytes ; Insulin ; Polymers ; Protamines ; Proteins ; Dextran Sulfate (9042-14-2)
Language	English
Publishing date	2004-07-21
Publishing country	United States
Document type	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
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Article ; 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 Volume 165, Issue 2, Page(s) 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 term(s)	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
Chemical Substances	Mucins
Language	English
Publishing date	2018-06-19
Publishing country	United States
Document type	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
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Article ; 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
Keywords	610 ; 541 ; 620
Subject code	612
Language	English
Publishing country	de
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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