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Modulation of α‑Chymotrypsin Conjugated to Magnetic Nanoparticles by the Non-Heating Low-Frequency Magnetic Field: Molecular Dynamics, Reaction Kinetics, and Spectroscopy Analysisстатья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 13 июля 2022 г.
- Авторы: Veselov M.M., Uporov I.V., Efremova M.V., Le-Deygen I.M., Prusov A.N., Shchetinin I.V., Savchenko A.G., Golovin Y.I., Kabanov A.V., Klyachko N.L.
- Журнал: ACS Omega
- Том: 7
- Номер: 24
- Год издания: 2022
- Первая страница: 20644
- Последняя страница: 20655
- Номер статьи: ao-2022-00704k
- DOI: 10.1021/acsomega.2c00704
- Аннотация: M.M. Veselov, I.V. Uporov, M.V. Efremova, I.M. Le-Deygen, A.N. Prusov, I.V. Shchetinin, A.G. Savchenko, Y.I. Golovin, A.V. Kabanov, N.L. Klyachko (2022). Modulation of α‑Chymotrypsin Conjugated to Magnetic Nanoparticles by the Non-Heating Low-Frequency Magnetic Field: Molecular Dynamics, Reaction Kinetics, and Spectroscopy Analysis. ACS Omega V. 7. No. 24. P. 20644−20655. Manuscript No.: ao-2022-00704k (10.1021/acsomega.2c00704); https://doi.org/10.1021/acsomega.2c00704 (published online June 7, 2022) IF 4.132 Russian Science Foundation grants 22-13-00261 and 20-63-46029. This work was supported in part by the Lomonosov Moscow State University (Registration Theme AAAA-A21-121011290089-4). The authors also acknowledge Lomonosov Moscow State University Development Program PNR 5.13.Enzymes conjugated to magnetic nanoparticles (MNPs) undergo changes in the catalytic activity of the non-heating low-frequency magnetic field (LFMF). We apply in silico simulations by molecular dynamics (MD) and in vitro spectroscopic analysis of the enzyme kinetics and secondary structure to study α-chymotrypsin (CT) conjugated to gold-coated iron oxide MNPs. The latter are functionalized by either carboxylic or amino group moieties to vary the points of enzyme attachment. The MD simulation suggests that application of the stretching force to the CT globule by its amino or carboxylic groups causes shrinkage of the substrate-binding site but little if any changes in the catalytic triad. Consistent with this, in CT conjugated to MNPs by either amino or carboxylic groups, LFMF alters the Michaelis–Menten constant but not the apparent catalytic constant kcat (= Vmax/[E]o). Irrespective of the point of conjugation to MNPs, the CT secondary structure was affected with nearly complete loss of α-helices and increase in the random structures in LFMF, as shown by attenuated total reflection Fourier transformed infrared spectroscopy. Both the catalytic activity and the protein structure of MNP-CT conjugates restored 3 h after the field exposure. We believe that such remotely actuated systems can find applications in advanced manufacturing, nanomedicine, and other areas.
- Добавил в систему: Клячко Наталья Львовна