Atomic Force Microscopy Study of the Effect of an Electric Field, Applied to a Pyramidal Structure, on Enzyme Biomolecules
The influence of an external constant strong electric field, formed using a pyramidal structure under a high electric potential, on an enzyme located near its apex, is studied. Horseradish peroxidase (HRP) is used as a model. In our experiments, a 27 kV direct current (DC) voltage was applied to two...
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MDPI AG
2022-11-01
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| Series: | Journal of Functional Biomaterials |
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| Online Access: | https://www.mdpi.com/2079-4983/13/4/234 |
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| author | Yuri D. Ivanov Vadim Y. Tatur Ivan D. Shumov Andrey F. Kozlov Anastasia A. Valueva Irina A. Ivanova Maria O. Ershova Nina D. Ivanova Igor N. Stepanov Andrei A. Lukyanitsa Vadim S. Ziborov |
| author_facet | Yuri D. Ivanov Vadim Y. Tatur Ivan D. Shumov Andrey F. Kozlov Anastasia A. Valueva Irina A. Ivanova Maria O. Ershova Nina D. Ivanova Igor N. Stepanov Andrei A. Lukyanitsa Vadim S. Ziborov |
| author_sort | Yuri D. Ivanov |
| collection | DOAJ |
| description | The influence of an external constant strong electric field, formed using a pyramidal structure under a high electric potential, on an enzyme located near its apex, is studied. Horseradish peroxidase (HRP) is used as a model. In our experiments, a 27 kV direct current (DC) voltage was applied to two electrodes with a conducting pyramidal structure attached to one of them. The enzyme particles were visualized by atomic force microscopy (AFM) after the adsorption of the enzyme from its 0.1 µM solution onto mica AFM substrates. It is demonstrated that after the 40 min exposure to the electric field, the enzyme forms extended structures on mica, while in control experiments compact HRP particles are observed. After the exposure to the electric field, the majority of mica-adsorbed HRP particles had a height of 1.2 nm (as opposed to 1.0 nm in the case of control experiments), and the contribution of higher (>2.0 nm) particles was also considerable. This indicates the formation of high-order HRP aggregates under the influence of an applied electric field. At that, the enzymatic activity of HRP against its substrate 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) remains unaffected. These results are important for studying macroscopic effects of strong electromagnetic fields on enzymes, as well as for the development of cellular structure models. |
| first_indexed | 2024-03-09T16:15:49Z |
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| id | doaj.art-6a8472d2bca2404196bfb21ba063a241 |
| institution | Directory Open Access Journal |
| issn | 2079-4983 |
| language | English |
| last_indexed | 2024-03-09T16:15:49Z |
| publishDate | 2022-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Journal of Functional Biomaterials |
| spelling | doaj.art-6a8472d2bca2404196bfb21ba063a2412023-11-24T15:49:56ZengMDPI AGJournal of Functional Biomaterials2079-49832022-11-0113423410.3390/jfb13040234Atomic Force Microscopy Study of the Effect of an Electric Field, Applied to a Pyramidal Structure, on Enzyme BiomoleculesYuri D. Ivanov0Vadim Y. Tatur1Ivan D. Shumov2Andrey F. Kozlov3Anastasia A. Valueva4Irina A. Ivanova5Maria O. Ershova6Nina D. Ivanova7Igor N. Stepanov8Andrei A. Lukyanitsa9Vadim S. Ziborov10Institute of Biomedical Chemistry, 119121 Moscow, RussiaFoundation of Perspective Technologies and Novations, 115682 Moscow, RussiaInstitute of Biomedical Chemistry, 119121 Moscow, RussiaInstitute of Biomedical Chemistry, 119121 Moscow, RussiaInstitute of Biomedical Chemistry, 119121 Moscow, RussiaInstitute of Biomedical Chemistry, 119121 Moscow, RussiaInstitute of Biomedical Chemistry, 119121 Moscow, RussiaFoundation of Perspective Technologies and Novations, 115682 Moscow, RussiaFoundation of Perspective Technologies and Novations, 115682 Moscow, RussiaFoundation of Perspective Technologies and Novations, 115682 Moscow, RussiaInstitute of Biomedical Chemistry, 119121 Moscow, RussiaThe influence of an external constant strong electric field, formed using a pyramidal structure under a high electric potential, on an enzyme located near its apex, is studied. Horseradish peroxidase (HRP) is used as a model. In our experiments, a 27 kV direct current (DC) voltage was applied to two electrodes with a conducting pyramidal structure attached to one of them. The enzyme particles were visualized by atomic force microscopy (AFM) after the adsorption of the enzyme from its 0.1 µM solution onto mica AFM substrates. It is demonstrated that after the 40 min exposure to the electric field, the enzyme forms extended structures on mica, while in control experiments compact HRP particles are observed. After the exposure to the electric field, the majority of mica-adsorbed HRP particles had a height of 1.2 nm (as opposed to 1.0 nm in the case of control experiments), and the contribution of higher (>2.0 nm) particles was also considerable. This indicates the formation of high-order HRP aggregates under the influence of an applied electric field. At that, the enzymatic activity of HRP against its substrate 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) remains unaffected. These results are important for studying macroscopic effects of strong electromagnetic fields on enzymes, as well as for the development of cellular structure models.https://www.mdpi.com/2079-4983/13/4/234atomic force microscopyhorseradish peroxidaseprotein aggregationapplied electric field |
| spellingShingle | Yuri D. Ivanov Vadim Y. Tatur Ivan D. Shumov Andrey F. Kozlov Anastasia A. Valueva Irina A. Ivanova Maria O. Ershova Nina D. Ivanova Igor N. Stepanov Andrei A. Lukyanitsa Vadim S. Ziborov Atomic Force Microscopy Study of the Effect of an Electric Field, Applied to a Pyramidal Structure, on Enzyme Biomolecules Journal of Functional Biomaterials atomic force microscopy horseradish peroxidase protein aggregation applied electric field |
| title | Atomic Force Microscopy Study of the Effect of an Electric Field, Applied to a Pyramidal Structure, on Enzyme Biomolecules |
| title_full | Atomic Force Microscopy Study of the Effect of an Electric Field, Applied to a Pyramidal Structure, on Enzyme Biomolecules |
| title_fullStr | Atomic Force Microscopy Study of the Effect of an Electric Field, Applied to a Pyramidal Structure, on Enzyme Biomolecules |
| title_full_unstemmed | Atomic Force Microscopy Study of the Effect of an Electric Field, Applied to a Pyramidal Structure, on Enzyme Biomolecules |
| title_short | Atomic Force Microscopy Study of the Effect of an Electric Field, Applied to a Pyramidal Structure, on Enzyme Biomolecules |
| title_sort | atomic force microscopy study of the effect of an electric field applied to a pyramidal structure on enzyme biomolecules |
| topic | atomic force microscopy horseradish peroxidase protein aggregation applied electric field |
| url | https://www.mdpi.com/2079-4983/13/4/234 |
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