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Dive into the research topics where L.Y. Filatova is active.

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Featured researches published by L.Y. Filatova.


Biochimie | 2010

LysK, the enzyme lysing Staphylococcus aureus cells: specific kinetic features and approaches towards stabilization.

L.Y. Filatova; Stephen C. Becker; David M. Donovan; Alexander K. Gladilin; Natalia L. Klyachko

LysK, the enzyme lysing cells of Staphylococcus aureus, can be considered as perspective antimicrobial agent. Knowledge of LysK properties and behavior would allow optimizing conditions of its storage as well as formulating strategy towards its stabilization. Reaction of LysK with substrate (suspension of autoclaved Staphylococcus aureus cells) has been found to be adequately described by the two-stage Michaelis-Menten kinetic scheme. Ionization of the enzyme and enzyme-substrate complex is important for revealing catalytic activity, which is controlled by two ionogenic groups with pK 6.0 and 9.6. Ionization energy of the group with pK 6.0 is of 30 kJ/mol, thus, pointing out on His residue; pK 9.6 might be attributed to metal ion or metal-bound water molecule. At temperatures lower than 40 degrees C, LysK stability depends on its concentration, pH and presence of low molecular weight additives. Results of electrophoresis under native and denaturing conditions as well as sedimentation analysis strongly suggest that aggregation is behind LysK inactivation. Decrease in the enzyme concentration, as well as addition of low molecular mass polyols (glycerol, sorbitol, sucrose, trehalose) and Ca(2+) cations resulted in an enhanced (more than 100 times) stability of LysK. Dramatic stability decline observed in a narrow temperature range (40-42 degrees C) was accompanied by changes in LysK secondary structure as confirmed by CD spectroscopy studies. According to computer modeling data, Cys and His residues and metal cation might play a crucial role for LysK catalytic activity. Our data on the enzyme activity in the presence of ethylenediaminetetraacetic acid and different metal cations confirmed the importance of metal cation in LysK catalysis.


Enzyme and Microbial Technology | 2015

Bacteriophage phi11 lysin: Physicochemical characterization and comparison with phage phi80α lysin.

L.Y. Filatova; David M. Donovan; Juli Foster-Frey; Vladimir G. Pugachev; Dmitrieva Nf; Tatiana Chubar; Natalia L. Klyachko; Alexander V. Kabanov

Phage lytic enzymes are promising antimicrobial agents. Lysins of phages phi11 (LysPhi11) and phi80α (LysPhi80α) can lyse (destroy) cells of antibiotic-resistant strains of Staphylococcus aureus. Stability of enzymes is one of the parameters making their practical use possible. The objectives of the study were to investigate the stability of lysins of phages phi11 and phi80α in storage and functioning conditions, to identify optimum storage conditions and causes of inactivation. Stability of the recombinant LysPhi11 and LysPhi80α was studied using turbidimetry. CD-spectroscopy, dynamic light scattering, and electrophoresis were used to identify causes of inactivation. At 37°C, pH 7.5 and concentration of NaCl not higher than 150mM, LysPhi11 molecules contain a high percentage of random coils (43%). However, in spite of this the enzyme has high activity (0.4-0.8OD600nms(-1)mg(-1)). In storage conditions (4°C and 22°C, pH 6.0-9.0, 10-500mM NaCl) LysPhi11 is inactivated by a monomolecular mechanism. The optimum storage conditions for LysPhi11 (4°C, pH 6.0-7.5, 10mM NaCl) were selected under which the time of the enzyme half-inactivation is 120-160 days. LysPhi80α stability is insufficient: at 37°C the enzyme loses half of its activity almost immediately; at 4°C and 22°C the time of half-inactivation of LysPhi80α varies in the range from several hours to 3 days. Despite the common properties in the manifestation of antistaphylococcal activity the kinetic behavior of the enzymes is different. LysPhi11 is a more promising candidate to be used as an antimicrobial agent.


Moscow University Chemistry Bulletin | 2016

Lytic enzymes of staphylococcal phages: Correlation between secondary structure and stability

L.Y. Filatova; David M. Donovan; J. A. Foster-Frey; V. G. Pugachev; Elena V. Kudryashova; Natalya L. Klyachko

Lytic enzymes of bacteriophages K, phi11, and phi80α can lyse (destroy) cells of antibiotic-resistant strains of Staphylococcus aureus, which makes these enzymes promising antimicrobial agents. The stability of recombinant lysins of phages K, phi11, and phi80α was investigated under the conditions of storage and functioning, and the correlation between the stability and the secondary structure of the enzymes was found. It has been shown that the lower the content of disordered structures in the enzyme molecules, the greater the stability (half-inactivation time) of the lysins. At the storage temperature, the beta-structural lysin of phage phi11 shows the highest stability, while the phage K lysin with an alpha-helical structure and the phi80α lysin with a disordered secondary structure are less stable.


Moscow University Chemistry Bulletin | 2014

An investigation of the physicochemical properties of both glutathione peroxidase I and its complexes with polyelectrolytes as promising agents for the treatment of diseases of the central nervous system

I. S. Panina; L.Y. Filatova; Alexander V. Kabanov; Natalia L. Klyachko

A study of the kinetics of the thermal inactivation of glutathione peroxidase I was carried out. Glutathione peroxidase is an enzyme that plays a key role in the antioxidant protection system of the body. It was shown that oligomeric glutathione peroxidase I is inactivated by a monomolecular mechanism (37°C, pH 7.0, the enzyme concentrations 0.3 and 1 mg/mL). An effective method for stabilizing the enzyme by polyelectrolytes of different natures was proposed.


Biochimie | 2013

Physicochemical characterization of the staphylolytic LysK enzyme in complexes with polycationic polymers as a potent antimicrobial.

L.Y. Filatova; David M. Donovan; Stephen C. Becker; Dmitry N. Lebedev; Anastasia D. Priyma; Helena V. Koudriachova; Alexander V. Kabanov; Natalia L. Klyachko


Applied Biochemistry and Biotechnology | 2016

A Chimeric LysK-Lysostaphin Fusion Enzyme Lysing Staphylococcus aureus Cells: a Study of Both Kinetics of Inactivation and Specifics of Interaction with Anionic Polymers

L.Y. Filatova; David M. Donovan; Nadiya T. Ishnazarova; Juli Foster-Frey; Stephen C. Becker; Vladimir G. Pugachev; N. G. Balabushevich; Dmitrieva Nf; Natalia L. Klyachko


Russian Chemical Reviews | 2018

Targeted delivery of anti-tuberculosis drugs to macrophages: targeting mannose receptors

L.Y. Filatova; Natalia L. Klyachko; Elena V. Kudryashova


Moscow University Chemistry Bulletin | 2018

Influence of Different Types of Block Copolymers on the Secondary Structure and Stability of the Staphylolytic Lysk Enzyme

L.Y. Filatova; David M. Donovan; I. A. Novozhilov; T. A. Chubar; N. G. Balabushevich; V. G. Pugachev; Natalya L. Klyachko


7th International Conference “Biomaterials and Nanobiomaterials: Recent Advances of Toxicology and Ecology Issues", Heraclion, Crete, Greece, 8-15 May 2016 | 2016

Bacterophage phi11 lysin: structure and inactivation kinetic

L.Y. Filatova; E.A. Zaitseva; David M. Donovan; Juli Foster-Frey; Vladimir G. Pugachev; Natalia L. Klyachko


7th International Conference “Biomaterials and Nanobiomaterials: Recent Advances of Toxicology and Ecology Issues", Heraclion, Crete, Greece, 8-15 May 2016 | 2016

A chimeric LysK-lysostaphin fusion enzyme lysing Staphylococcus aureus cells: kinetic peculiarities of inactivation and specifics of interaction with block-copolymers of poly-L-glutamic acid and polyethylene glycol

L.Y. Filatova; E.A. Zaitseva; David M. Donovan; N.T. Ishnazarova; Juli Foster-Frey; Vladimir G. Pugachev; Natalia L. Klyachko

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David M. Donovan

United States Department of Agriculture

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Alexander V. Kabanov

University of North Carolina at Chapel Hill

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Vladimir G. Pugachev

State Research Center of Virology and Biotechnology VECTOR

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Juli Foster-Frey

United States Department of Agriculture

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E. Efremenko

Moscow State University

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