The Effect of Incubation near an Inversely Oriented Square Pyramidal Structure on Adsorption Properties of Horseradish Peroxidase
Source abstract
Abstract
The incubation of a solution of horseradish peroxidase (HRP) enzyme either below the apex or near the base of an inversely oriented square pyramid (inverted square pyramid; ISP) has been found to influence the enzyme’s aggregation and adsorption properties. The HRP enzyme is used herein as a model object due to its importance in analytical chemistry applications. Atomic force microscopy (AFM) is employed to investigate the HRP’s adsorption on mica substrates at the single-molecule level. Conventional spectrophotometry is used in parallel as a reference method for the determination of the HRP’s enzymatic activity. Using AFM, we reveal a significant change in the adsorption properties of HRP on mica substrates after the incubation of the HRP solutions either above the base or below the apex of the ISP in comparison with the control HRP solution. The same situation is observed after the incubation of the enzyme solution above the center of the ISP’s base. Here, the enzymatic activity of HRP remained unaffected in both cases. Since pyramidal structures of positive and inverted orientation are employed in biosensor devices, it is important to take into account the results obtained herein in the development of highly sensitive biosensor systems, in which pyramidal structures are employed as sensor (such as AFM probes) or construction elements.
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Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · Molecular Junctions and Nanostructures · Force Microscopy Techniques and Applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Institute of Biomedical Chemistry, Pogodinskaya Str., 10 Build. 8, Moscow 119121, Russia
Joint Institute for High Temperatures of the Russian Academy of Sciences, Moscow 125412, Russia
Foundation of Perspective Technologies and Novations, Moscow 115682, Russia
Moscow State Academy of Veterinary Medicine and Biotechnology Named after Skryabin, Moscow 109472, Russia
Funding
The Ministry of Science and Higher Education of the Russian Federation within the framework of state support for the creation and development of World-Class Research Centers “Digital biodesign and personalized healthcare”
References (36)
Show source-provided references
1. Single molecule enzymology finds its stride10.2144/000114337 ↗
2. Single-Molecule Enzymology for Diagnostics: Profiling Alkaline Phosphatase Activity in Clinical Samples10.1002/cbic.202100358 ↗
3. Structural and Dynamic Characterization of Biochemical Processes by Atomic Force Microscopy10.1007/978-1-61779-261-8_6 ↗
4. Single-molecule enzymology10.1074/jbc.274.23.15967 ↗
5. AFM study of cytochrome CYP102A1 oligomeric state10.1039/c2sm07333a ↗
6. Atomic force microscopy visualization and measurement of the activity and physicochemical properties of single monomeric and oligomeric enzymes10.1134/S000635091105006X ↗
7. Atomic Force Microscopy Study of Protein–Protein Interactions in the Cytochrome CYP11A1 (P450scc)-Containing Steroid Hydroxylase System10.1007/s11671-010-9809-5 ↗
8. Ultrasensitive nanowire-based detection of HCVcoreAg in the serum using a microwave generator10.1039/C8AY00495A ↗
9. Multiplexed electrical detection of cancer markers with nanowire sensor arrays10.1038/nbt1138 ↗
10. Electrical detection of single viruses10.1073/pnas.0406159101 ↗
11. Tintelott, M., Pachauri, V., Ingebrandt, S., and Vu, X.T. (2021). Process variability in top-down fabrication of silicon nanowire-based biosensor arrays. Sensors, 21.10.3390/s21155153 ↗
12. Single-molecule nanopore enzymology10.1098/rstb.2016.0230 ↗
13. Kolmogorov, M., Kennedy, E., Dong, Z., Timp, G., and Pevzner, P.A. (2017). Single-molecule protein identification by sub-nanopore sensors. PLoS Comput. Biol., 13.10.1371/journal.pcbi.1005356 ↗
14. Signal amplification of SiO2 nanoparticle loaded horseradish peroxidase for colorimetric detection of lead ions in water10.1016/j.saa.2021.120342 ↗
15. Nayak, S., Kale, P., and Balasubramanian, P. (2020). Inhibition assays of horseradish peroxidase by hexavalent chromium and other heavy metals. Int. J. Environ. Anal. Chem.10.1080/03067319.2020.1776864 ↗
16. Amperometric Flow-Injection Analysis of Phenols Induced by Reactive Oxygen Species Generated under Daylight Irradiation of Titania Impregnated with Horseradish Peroxidase10.1021/acs.analchem.9b04617 ↗
17. Simultaneous transfer of noble metals and three-dimensional micro- and nanopatterns onto zein for fabrication of nanophotonic platforms10.1007/s10853-015-9699-0 ↗
18. Disposable gold coated pyramidal SERS sensor on the plastic platform10.1364/OE.24.000724 ↗
19. Miniaturized real-time monitoring system for l-lactate and glucose using microfabricated multi-enzyme sensors10.1016/S0956-5663(00)00087-7 ↗
20. Tuning localized plasmons in nanostructured substrates for surface-enhanced Raman scattering10.1364/OPEX.14.000847 ↗
21. Electromagnetic properties of the great pyramid: First multipole resonances and energy concentration10.1063/1.5026556 ↗
22. AFM study of changes in properties of horseradish peroxidase after incubation of its solution near a pyramidal structure10.1038/s41598-021-89377-z ↗
23. Atomic Force Microscopy of Protein Complexes
24. Effect of ampicillin on adhesive properties of bacteria examined by atomic force microscopy10.1016/j.micron.2018.05.005 ↗
25. Ivanov, Y., Tatur, V., Pleshakova, T., Shumov, I., Kozlov, A., Valueva, A., Ivanova, I., Ershova, M., Ivanova, N., and Repnikov, V. (2021). Effect of Spherical Elements of Biosensors and Bioreactors on the Physicochemical Properties of a Peroxidase Protein. Polymers, 13.10.3390/polym13101601 ↗
26. AFM imaging of protein aggregation in studying the impact of knotted electromagnetic field on a peroxidase10.1038/s41598-020-65888-z ↗
27. AFM study of membrane proteins, cytochrome P450 2B4, and NADPH–Cytochrome P450 reductase and their complex formation10.1006/abbi.1999.1412 ↗
28. Pleshakova, T.O., Kaysheva, A.L., Shumov, I.D., Ziborov, V.S., Bayzyanova, J.M., Konev, V.A., Uchaikin, V.F., Archakov, A.I., and Ivanov, Y.D. (2019). Detection of hepatitis C virus core protein in serum using aptamer-functionalized AFM chips. Micromachines, 10.10.3390/mi10020129 ↗
29. Irreversible chemical AFM-based fishing for detection of low-copied proteins10.1134/S1990750813010071 ↗
30. pH-Dependent properties of a mutant horseradish peroxidase isoenzyme C in which Arg38 has been replaced with lysine10.1111/j.1432-1033.1994.01029.x ↗
31. (2022, February 18). Enzymatic Assay of Peroxidase (EC 1.11.1.7) 2,2′-Azino-Bis(3-Ethylbenzthiazoline-6-Sulfonic Acid) as a Substrate Sigma Prod. No. P-6782. Available online: https://www.sigmaaldrich.com/RU/en/technical-documents/protocol/protein-biology/enzyme-activity-assays/enzymatic-assay-of-peroxidase-abts-as-substrate.
32. Ivanov, Y.D., Malsagova, K.A., Bukharina, N.S., Vesnin, S.G., Usanov, S.A., Tatur, V.Y., Lukyanitsa, A.A., Ivanova, N.D., Konev, V.A., and Ziborov, V.S. (2022). Radiothermometric Study of the Effect of Amino Acid Mutation on the Characteristics of the Enzymatic System. Diagnostics, 12.10.3390/diagnostics12040943 ↗
33. Pershin, S.M. (2022, April 07). A New of the Action of EMF on Water/Aqueous Solutions, Taking into Account the Quantum Differences of the Ortho/Para of Spin Isomers of H2O. Online Biophysical Blog. Available online: http://www.biophys.ru/archive/sarov2013/proc-p17.pdf.
34. Electromagnetic properties of the pyramids from the photonics position10.1007/s11182-020-01904-z ↗
35. Calculation and modeling of monostatic EPR of simple bodies
36. Campanile near-field probes fabricated by nanoimprint lithography on the facet of an optical fiber10.1038/s41598-017-01871-5 ↗