9 results on '"Nesmeyanova, Valentina S."'
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2. Natural IgG against S-Protein and RBD of SARS-CoV-2 Do Not Bind and Hydrolyze DNA and Are Not Autoimmune
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Timofeeva, Anna M., primary, Sedykh, Sergey E., additional, Ermakov, Evgeny A., additional, Matveev, Andrey L., additional, Odegova, Eva I., additional, Sedykh, Tatiana A., additional, Shcherbakov, Dmitry N., additional, Merkuleva, Iuliia A., additional, Volosnikova, Ekaterina A., additional, Nesmeyanova, Valentina S., additional, Tikunova, Nina V., additional, and Nevinsky, Georgy A., additional
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- 2022
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3. Antibodies to the Spike Protein Receptor-Binding Domain of SARS-CoV-2 at 4–13 Months after COVID-19
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Kolosova, Evgeniia A., primary, Shaprova, Olga N., additional, Shanshin, Daniil V., additional, Nesmeyanova, Valentina S., additional, Merkuleva, Iuliia A., additional, Belenkaya, Svetlana V., additional, Isaeva, Anastasiya A., additional, Nikitin, Artem O., additional, Volosnikova, Ekaterina A., additional, Nikulina, Yuliya A., additional, Nikonorova, Marina A., additional, Shcherbakov, Dmitry N., additional, and Elchaninova, Svetlana A., additional
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- 2022
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4. Are Hamsters a Suitable Model for Evaluating the Immunogenicity of RBD-Based Anti-COVID-19 Subunit Vaccines?
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Merkuleva, Iuliia A., primary, Shcherbakov, Dmitry N., additional, Borgoyakova, Mariya B., additional, Isaeva, Anastasiya A., additional, Nesmeyanova, Valentina S., additional, Volkova, Natalia V., additional, Aripov, Vazirbek S., additional, Shanshin, Daniil V., additional, Karpenko, Larisa I., additional, Belenkaya, Svetlana V., additional, Kazachinskaia, Elena I., additional, Volosnikova, Ekaterina A., additional, Esina, Tatiana I., additional, Sergeev, Alexandr A., additional, Titova, Kseniia A., additional, Konyakhina, Yulia V., additional, Zaykovskaya, Anna V., additional, Pyankov, Oleg V., additional, Kolosova, Evgeniia A., additional, Viktorina, Olesya E., additional, Shelemba, Arseniya A., additional, Rudometov, Andrey P., additional, and Ilyichev, Alexander A., additional
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- 2022
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5. Structure‐ and Interaction‐Based Design of Anti‐SARS‐CoV‐2 Aptamers
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Mironov, Vladimir, primary, Shchugoreva, Irina A., additional, Artyushenko, Polina V., additional, Morozov, Dmitry, additional, Borbone, Nicola, additional, Oliviero, Giorgia, additional, Zamay, Tatiana N., additional, Moryachkov, Roman V., additional, Kolovskaya, Olga S., additional, Lukyanenko, Kirill A., additional, Song, Yanling, additional, Merkuleva, Iuliia A., additional, Zabluda, Vladimir N., additional, Peters, Georgy, additional, Koroleva, Lyudmila S., additional, Veprintsev, Dmitry V., additional, Glazyrin, Yury E., additional, Volosnikova, Ekaterina A., additional, Belenkaya, Svetlana V., additional, Esina, Tatiana I., additional, Isaeva, Anastasiya A., additional, Nesmeyanova, Valentina S., additional, Shanshin, Daniil V., additional, Berlina, Anna N., additional, Komova, Nadezhda S., additional, Svetlichnyi, Valery A., additional, Silnikov, Vladimir N., additional, Shcherbakov, Dmitriy N., additional, Zamay, Galina S., additional, Zamay, Sergey S., additional, Smolyarova, Tatyana, additional, Tikhonova, Elena P., additional, Chen, Kelvin H.‐C., additional, Jeng, U‐Ser, additional, Condorelli, Gerolama, additional, Franciscis, Vittorio, additional, Groenhof, Gerrit, additional, Yang, Chaoyong, additional, Moskovsky, Alexander A., additional, Fedorov, Dmitri G., additional, Tomilin, Felix N., additional, Tan, Weihong, additional, Alexeev, Yuri, additional, Berezovski, Maxim V., additional, and Kichkailo, Anna S., additional
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- 2022
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6. Self-Assembled Particles Combining SARS-CoV-2 RBD Protein and RBD DNA Vaccine Induce Synergistic Enhancement of the Humoral Response in Mice
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Borgoyakova, Mariya B., primary, Karpenko, Larisa I., additional, Rudometov, Andrey P., additional, Volosnikova, Ekaterina A., additional, Merkuleva, Iuliia A., additional, Starostina, Ekaterina V., additional, Zadorozhny, Alexey M., additional, Isaeva, Anastasiya A., additional, Nesmeyanova, Valentina S., additional, Shanshin, Daniil V., additional, Baranov, Konstantin O., additional, Volkova, Natalya V., additional, Zaitsev, Boris N., additional, Orlova, Lyubov A., additional, Zaykovskaya, Anna V., additional, Pyankov, Oleg V., additional, Danilenko, Elena D., additional, Bazhan, Sergei I., additional, Shcherbakov, Dmitry N., additional, Taranin, Alexander V., additional, and Ilyichev, Alexander A., additional
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- 2022
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7. Comparative Immunogenicity of the Recombinant Receptor-Binding Domain of Protein S SARS-CoV-2 Obtained in Prokaryotic and Mammalian Expression Systems
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Merkuleva, Iuliia A., primary, Shcherbakov, Dmitry N., additional, Borgoyakova, Mariya B., additional, Shanshin, Daniil V., additional, Rudometov, Andrey P., additional, Karpenko, Larisa I., additional, Belenkaya, Svetlana V., additional, Isaeva, Anastasiya A., additional, Nesmeyanova, Valentina S., additional, Kazachinskaia, Elena I., additional, Volosnikova, Ekaterina A., additional, Esina, Tatiana I., additional, Zaykovskaya, Anna V., additional, Pyankov, Oleg V., additional, Borisevich, Sophia S., additional, Shelemba, Arseniya A., additional, Chikaev, Anton N., additional, and Ilyichev, Alexander A., additional
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- 2022
- Full Text
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8. Structure‐ and Interaction‐Based Design of Anti‐SARS‐CoV‐2 Aptamers
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Vladimir Mironov, Irina A. Shchugoreva, Polina V. Artyushenko, Dmitry Morozov, Nicola Borbone, Giorgia Oliviero, Tatiana N. Zamay, Roman V. Moryachkov, Olga S. Kolovskaya, Kirill A. Lukyanenko, Yanling Song, Iuliia A. Merkuleva, Vladimir N. Zabluda, Georgy Peters, Lyudmila S. Koroleva, Dmitry V. Veprintsev, Yury E. Glazyrin, Ekaterina A. Volosnikova, Svetlana V. Belenkaya, Tatiana I. Esina, Anastasiya A. Isaeva, Valentina S. Nesmeyanova, Daniil V. Shanshin, Anna N. Berlina, Nadezhda S. Komova, Valery A. Svetlichnyi, Vladimir N. Silnikov, Dmitriy N. Shcherbakov, Galina S. Zamay, Sergey S. Zamay, Tatyana Smolyarova, Elena P. Tikhonova, Kelvin H.‐C. Chen, U‐Ser Jeng, Gerolama Condorelli, Vittorio Franciscis, Gerrit Groenhof, Chaoyong Yang, Alexander A. Moskovsky, Dmitri G. Fedorov, Felix N. Tomilin, Weihong Tan, Yuri Alexeev, Maxim V. Berezovski, Anna S. Kichkailo, Mironov, Vladimir, Shchugoreva, Irina A., Artyushenko, Polina V., Morozov, Dmitry, Borbone, Nicola, Oliviero, Giorgia, Zamay, Tatiana N., Moryachkov, Roman V., Kolovskaya, Olga S., Lukyanenko, Kirill A., Song, Yangling, Merkuleva, Iuliia A., Zabluda, Vladimir N., Peters, Georgy, Koroleva, Lyudmila S., Veprintsev, Dmitry V., Glazyrin, Yury E., Volosnikova, Ekaterina A., Belenkaya, Svetlana V., Esina, Tatiana I., Isaeva, Anastasiya A., Nesmeyanova, Valentina S., Shanshin, Daniil V., Berlina, Anna N., Komova, Nadezhda S., Svetlichnyi, Valery A., Silnikov, Vladimir N., Shcherbakov, Dmitriy N., Zamay, Galina S., Zamay, Sergey S., Smolyarova, Tatyana, Tikhonova, Elena P., Chen, Kelvin H. -C., Jeng, U-Ser, Condorelli, Gerolama, de Franciscis, Vittorio, Groenhof, Gerrit, Yang, Chaoyong, Moskovsky, Alexander A., Fedorov, Dmitri G., Tomilin, Felix N., Tan, Weihong, Alexeev, Yuri, Berezovski, Maxim V., and Kichkailo, Anna S
- Subjects
oligonukleotidit ,aptamers, fragment molecular orbitals method, molecular dynamics, SARS-CoV-2, SAXS ,fragment molecular orbitals method ,SARS-CoV-2 ,SELEX Aptamer Technique ,Organic Chemistry ,aptamers ,SARS-CoV-2-virus ,COVID-19 ,SAXS ,General Chemistry ,Aptamers, Nucleotide ,Molecular Dynamics Simulation ,laskennallinen kemia ,molecular dynamics ,Catalysis ,lääkesuunnittelu ,Molecular Docking Simulation ,SARS-CoV-2, белки ,Spike Glycoprotein, Coronavirus ,Humans ,дизайн аптамеров ,molekyylidynamiikka ,proteiinit - Abstract
Aptamer selection against novel infections is a complicated and time-consuming approach. Synergy can be achieved by using computational methods together with experimental procedures. This study aims to develop a reliable methodology for a rational aptamer in silico et vitro design. The new approach combines multiple steps: (1) Molecular design, based on screening in a DNA aptamer library and directed mutagenesis to fit the protein tertiary structure; (2) 3D molecular modeling of the target; (3) Molecular docking of an aptamer with the protein; (4) Molecular dynamics (MD) simulations of the complexes; (5) Quantum-mechanical (QM) evaluation of the interactions between aptamer and target with further analysis; (6) Experimental verification at each cycle for structure and binding affinity by using small-angle X-ray scattering, cytometry, and fluorescence polarization. By using a new iterative design procedure, structure- and interaction-based drug design (SIBDD), a highly specific aptamer to the receptor-binding domain of the SARS-CoV-2 spike protein, was developed and validated. The SIBDD approach enhances speed of the high-affinity aptamers development from scratch, using a target protein structure. The method could be used to improve existing aptamers for stronger binding. This approach brings to an advanced level the development of novel affinity probes, functional nucleic acids. It offers a blueprint for the straightforward design of targeting molecules for new pathogen agents and emerging variants.
- Published
- 2022
9. Structure- and Interaction-Based Design of Anti-SARS-CoV-2 Aptamers.
- Author
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Mironov V, Shchugoreva IA, Artyushenko PV, Morozov D, Borbone N, Oliviero G, Zamay TN, Moryachkov RV, Kolovskaya OS, Lukyanenko KA, Song Y, Merkuleva IA, Zabluda VN, Peters G, Koroleva LS, Veprintsev DV, Glazyrin YE, Volosnikova EA, Belenkaya SV, Esina TI, Isaeva AA, Nesmeyanova VS, Shanshin DV, Berlina AN, Komova NS, Svetlichnyi VA, Silnikov VN, Shcherbakov DN, Zamay GS, Zamay SS, Smolyarova T, Tikhonova EP, Chen KH, Jeng US, Condorelli G, de Franciscis V, Groenhof G, Yang C, Moskovsky AA, Fedorov DG, Tomilin FN, Tan W, Alexeev Y, Berezovski MV, and Kichkailo AS
- Subjects
- Humans, Molecular Docking Simulation, Molecular Dynamics Simulation, SARS-CoV-2, SELEX Aptamer Technique, Spike Glycoprotein, Coronavirus, Aptamers, Nucleotide chemistry, COVID-19
- Abstract
Aptamer selection against novel infections is a complicated and time-consuming approach. Synergy can be achieved by using computational methods together with experimental procedures. This study aims to develop a reliable methodology for a rational aptamer in silico et vitro design. The new approach combines multiple steps: (1) Molecular design, based on screening in a DNA aptamer library and directed mutagenesis to fit the protein tertiary structure; (2) 3D molecular modeling of the target; (3) Molecular docking of an aptamer with the protein; (4) Molecular dynamics (MD) simulations of the complexes; (5) Quantum-mechanical (QM) evaluation of the interactions between aptamer and target with further analysis; (6) Experimental verification at each cycle for structure and binding affinity by using small-angle X-ray scattering, cytometry, and fluorescence polarization. By using a new iterative design procedure, structure- and interaction-based drug design (SIBDD), a highly specific aptamer to the receptor-binding domain of the SARS-CoV-2 spike protein, was developed and validated. The SIBDD approach enhances speed of the high-affinity aptamers development from scratch, using a target protein structure. The method could be used to improve existing aptamers for stronger binding. This approach brings to an advanced level the development of novel affinity probes, functional nucleic acids. It offers a blueprint for the straightforward design of targeting molecules for new pathogen agents and emerging variants., (© 2022 Wiley-VCH GmbH.)
- Published
- 2022
- Full Text
- View/download PDF
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