Alexey V. Shnitko
@new.skoltech.ru
Center for Engineering Physics
Skolkovo Institute of Science and Technology
1
Scopus Publications
Scopus Publications
- Lysozyme binding with amikacin and levofloxacin studied by tritium probe, fluorescence spectroscopy and molecular docking
Hanna S. Skrabkova, Maria G. Chernysheva, Timur M. Baygildiev, Alexey V. Shnitko, Alexandra V. Kasperovich, Tolganay B. Egorova, Gennadii A. Badun, Alexander M. Arutyunyan, Alexander L. Ksenofontov, and Igor A. Rodin
Elsevier BV - Structural peculiarities of lysozyme-graphene oxide adsorption complexes
Vitalii A. Bunyaev, Alexey V. Shnitko, Maria G. Chernysheva, Alexander L. Ksenofontov, and Gennadii A. Badun
Informa UK Limited
Abstract Lysozyme adsorption complexes with graphene oxide (GO) and reduced GO were studied by means of radiotracer method using tritium as a label. The experiment includes adsorption study, with amount and enzymatic activity control, and revealing structural peculiarities of lysozyme adsorbed on graphene oxide surface by analysis of tritium distribution in the amino acid residues after the bombardment with atomic tritium. Experimental and molecular docking results suggested that lysozyme adsorbs directly on GO by formation of bonds between GO surface and Cys6 and Arg128 that contribute to formation conformation, in which aromatic residues forms π-π bonds with GO surface, and positively charged amino acid residues bind with O-containing groups of GO via electrostatic attraction. In the follow-up layers lysozyme molecules interact with each other that result in changes and adsorbed lysozyme molecules resulting in changes in protein structure. Such changes are not critically significant but lead to increase of availability of an active site of the enzyme for binding with a substrate after the desorption from the multilayer. - Peculiarities of alkylamidopropyldimethylbenzylammonium (Miramistin) in the relationship to lysozyme in comparison with quaternary ammonium surfactants: Coadsorption at the interfaces, enzymatic activity and molecular docking
Maria G. Chernysheva, Alexey V. Shnitko, Hanna S. Skrabkova, and Gennadii A. Badun
Elsevier BV - Kinetic analysis as an approach to studying specific features of lysozyme—pluronic complexes
A. V. Shnitko, M. G. Chernysheva, P. A. Levashov, and G. A. Badun
Springer Science and Business Media LLC - Lysozyme-dalargin self-organization at the aqueous-air and liquid-liquid interfaces
Maria G. Chernysheva, Alexandra V. Kasperovich, Hanna S. Skrabkova, Alexey V. Snitko, Alexander M. Arutyunyan, and Gennadii A. Badun
Elsevier BV - Structural peculiarities of lysozyme – PLURONIC complexes at the aqueous-air and liquid-liquid interfaces and in the bulk of aqueous solution
Maria G. Chernysheva, Alexey V. Shnitko, Alexander L. Ksenofontov, Alexander M. Arutyunyan, Maxim V. Petoukhov, and Gennadii A. Badun
Elsevier BV - Pluronics and Brij-35 Reduce the Bacteriolytic Activity of Lysozyme
A. V. Shnitko, M. G. Chernysheva, S. A. Smirnov, P. A. Levashov, and G. A. Badun
Allerton Press - Lysozyme-surfactant adsorption at the aqueous-air and aqueous-organic liquid interfaces as studied by tritium probe
Maria G. Chernysheva, Gennadii A. Badun, Alexey V. Shnitko, Valentina I. Petrova, and Alexander L. Ksenofontov
Elsevier BV - Competitive adsorption of lysozyme and non-ionic surfactants (Brij-35 and pluronic P123) from a mixed solution at water-air and water-xylene interfaces
Maria G. Chernysheva, Alexey V. Shnitko, Oxana A. Soboleva, and Gennadii A. Badun
Springer Science and Business Media LLC