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The Effect of a Dodecahedron-Shaped Structure on the Properties of an Enzyme.

作者信息

Ivanov Yuri D, Tatur Vadim Y, Shumov Ivan D, Kozlov Andrey F, Valueva Anastasia A, Ivanova Irina A, Ershova Maria O, Ivanova Nina D, Stepanov Igor N, Lukyanitsa Andrei A, Ziborov Vadim S

机构信息

Institute of Biomedical Chemistry, Pogodinskaya Str., 10 Build. 8, 119121 Moscow, Russia.

Joint Institute for High Temperatures of the Russian Academy of Sciences, 125412 Moscow, Russia.

出版信息

J Funct Biomater. 2022 Sep 28;13(4):166. doi: 10.3390/jfb13040166.


DOI:10.3390/jfb13040166
PMID:36278635
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9590084/
Abstract

In this research, the influence of a dodecahedron-shaped structure on the adsorption behavior of a horseradish peroxidase (HRP) enzyme glycoprotein onto mica substrates was studied. In the experiments, samples of an aqueous HRP solution were incubated at various distances (0.03 m, 2 m, 5 m, and control at 20 m) from the dodecahedron surface. After the incubation, the direct adsorption of HRP onto mica substrates immersed in the solutions was performed, and the mica-adsorbed HRP particles were visualized via atomic force microscopy (AFM). The effect of the increased HRP aggregation was only observed after the incubation of the enzyme solution at the 2 m distance from the dodecahedron. In addition, with respect to the control sample, spectrophotometric measurements revealed no change in the HRP enzymatic activity after the incubation at any of the distances studied. The results reported herein can be of use in the modeling of the possible influences of various spatial structures on biological objects in the development of biosensors and other electronic equipment.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/95d46aec37cb/jfb-13-00166-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/9b5d7388de9a/jfb-13-00166-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/47127dd5e55d/jfb-13-00166-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/1726467bfd85/jfb-13-00166-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/50da62bb5130/jfb-13-00166-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/db3fb5787a1a/jfb-13-00166-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/95d46aec37cb/jfb-13-00166-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/9b5d7388de9a/jfb-13-00166-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/47127dd5e55d/jfb-13-00166-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/1726467bfd85/jfb-13-00166-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/50da62bb5130/jfb-13-00166-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/db3fb5787a1a/jfb-13-00166-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c9e/9590084/95d46aec37cb/jfb-13-00166-g006.jpg

相似文献

[1]
The Effect of a Dodecahedron-Shaped Structure on the Properties of an Enzyme.

J Funct Biomater. 2022-9-28

[2]
AFM study of changes in properties of horseradish peroxidase after incubation of its solution near a pyramidal structure.

Sci Rep. 2021-5-10

[3]
The Effect of a Rotating Cone on Horseradish Peroxidase Aggregation on Mica Revealed by Atomic Force Microscopy.

Micromachines (Basel). 2022-11-10

[4]
Atomic Force Microscopy Study of the Temperature and Storage Duration Dependencies of Horseradish Peroxidase Oligomeric State.

Biomedicines. 2022-10-20

[5]
Atomic Force Microscopy Study of the Effect of an Electric Field, Applied to a Pyramidal Structure, on Enzyme Biomolecules.

J Funct Biomater. 2022-11-10

[6]
Effect of Spherical Elements of Biosensors and Bioreactors on the Physicochemical Properties of a Peroxidase Protein.

Polymers (Basel). 2021-5-15

[7]
Stopped Flow of Glycerol Induces the Enhancement of Adsorption and Aggregation of HRP on Mica.

Micromachines (Basel). 2023-5-10

[8]
AFM and FTIR Investigation of the Effect of Water Flow on Horseradish Peroxidase.

Molecules. 2021-1-9

[9]
Atomic Force Microscopy Study of the Long-Term Effect of the Glycerol Flow, Stopped in a Coiled Heat Exchanger, on Horseradish Peroxidase.

Micromachines (Basel). 2024-4-4

[10]
AFM Investigation of the Influence of Steam Flow through a Conical Coil Heat Exchanger on Enzyme Properties.

Micromachines (Basel). 2022-11-22

引用本文的文献

[1]
Incubation of Horseradish Peroxidase near 50 Hz AC Equipment Promotes Its Disaggregation and Enzymatic Activity.

Micromachines (Basel). 2025-3-19

[2]
Stopped Flow of Glycerol Induces the Enhancement of Adsorption and Aggregation of HRP on Mica.

Micromachines (Basel). 2023-5-10

[3]
The Effect of a Rotating Cone on Horseradish Peroxidase Aggregation on Mica Revealed by Atomic Force Microscopy.

Micromachines (Basel). 2022-11-10

本文引用的文献

[1]
The effect of radio frequency heating on the inactivation and structure of horseradish peroxidase.

Food Chem. 2023-1-1

[2]
Facile synthesis of ZIF-67 derived dodecahedral C/NiCOS with broadband microwave absorption performance.

Nanoscale. 2022-7-28

[3]
Effect of Spherical Elements of Biosensors and Bioreactors on the Physicochemical Properties of a Peroxidase Protein.

Polymers (Basel). 2021-5-15

[4]
AFM study of changes in properties of horseradish peroxidase after incubation of its solution near a pyramidal structure.

Sci Rep. 2021-5-10

[5]
AFM and FTIR Investigation of the Effect of Water Flow on Horseradish Peroxidase.

Molecules. 2021-1-9

[6]
Investigation of static magnetic field effect on horseradish peroxidase enzyme activity and stability in enzymatic oxidation process.

Int J Biol Macromol. 2021-2-15

[7]
The Adenovirus Dodecahedron: Beyond the Platonic Story.

Viruses. 2020-7-2

[8]
AFM Imaging of Protein Aggregation in Studying the Impact of Knotted Electromagnetic Field on A Peroxidase.

Sci Rep. 2020-6-2

[9]
3D ZnInS nanosheets decorated ZnCdS dodecahedral cages as multifunctional signal amplification matrix combined with electroactive/photoactive materials for dual mode electrochemical - photoelectrochemical detection of bovine hemoglobin.

Biosens Bioelectron. 2020-7-1

[10]
Spatially nanoscale-controlled functional surfaces toward efficient bioactive platforms.

J Mater Chem B. 2015-7-14

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