scholarly journals Investigation of the Influence of Liquid Motion in a Flow-based System on an Enzyme Aggregation State with an Atomic Force Microscopy Sensor: The Effect of Water Flow

2020 ◽  
Vol 10 (13) ◽  
pp. 4560 ◽  
Author(s):  
Yuri D. Ivanov ◽  
Tatyana O. Pleshakova ◽  
Ivan D. Shumov ◽  
Andrey F. Kozlov ◽  
Tatyana S. Romanova ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Enzymatic Activity ◽  
Liquid Flow ◽  
Flow Section ◽  
Liquid Motion ◽  
Aggregation State ◽  
Measuring Cell ◽  
Force Microscopy ◽  
Atomic Force ◽  
Solution Studies

The influence of liquid motion in flow-based systems on the aggregation state of an enzyme and on its enzymatic activity was studied, with horseradish peroxidase (HRP) as an example. Our experiments were carried out in a setup modeling the flow section of the biosensor communication with a measuring cell containing a protein solution. Studies were conducted for a biosensor measuring cell located along the axis of a spiral-moving liquid flow. The aggregation state of the protein was determined with an atomic force microscopy-based sensor (AFM sensor). It has been demonstrated that upon flowing of water through silicone biosensor communications, an increased aggregation of HRP protein was observed, but, at the same time, its enzymatic activity did not change. Our results obtained herein are useful in the development of models describing the influence of liquid flow in biosensor communications on the properties of enzymes and other proteins. This is particularly important for the development of serologic protein biosensors, which are beginning to be used for the early diagnosis of oncological diseases (such as brain cancer, prostate cancer, breast cancer etc.). The results obtained herein should also be taken into account when considering possible changes in hemodynamics due to increased protein aggregation.

scholarly journals Investigation of the Influence of Liquid Motion in a Flow-Based System on an Enzyme Aggregation State with an Atomic Force Microscopy Sensor: The Effect of Glycerol Flow

2020 ◽  
Vol 10 (14) ◽  
pp. 4825 ◽  
Author(s):  
Vadim S. Ziborov ◽  
Tatyana O. Pleshakova ◽  
Ivan D. Shumov ◽  
Andrey F. Kozlov ◽  
Irina A. Ivanova ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Thermal Stabilization ◽  
Glycerol Solution ◽  
Experimental Setup ◽  
Liquid Motion ◽  
Hydrodynamic Models ◽  
Aggregation State ◽  
Measuring Cell ◽  
Force Microscopy ◽  
Atomic Force

Atomic force microscopy is employed to study the influence of the motion of a glycerol solution through a coiled (spiral-wound) polymeric communication pipe on the aggregation state of a protein, with the example of a horseradish peroxidase (HRP) enzyme. The measuring cell with the buffered solution of the protein was placed within the experimental setup over the pipe coil, through which glycerol was pumped. It is demonstrated that, in such a system, the flow of a non-aqueous liquid (glycerol) leads to a change in the physicochemical properties of a protein, whose solution was incubated in the measuring cell placed over the coil. Namely, changes in both the adsorbability onto mica and the aggregation state of the model HRP protein were observed. As glycerol-containing liquids are commonly used in biosensor operations, the results reported herein can be useful to the development of biosensor systems, in which polymeric communications are employed in sample delivery and thermal stabilization systems. The data obtained herein can also be of use for the development of specified hydrodynamic models.

GROWTH HILLOCKS ON THE {100} FACES OF L-ARGININE PHOSPHATE MONOHYDRATE SINGLE CRYSTALS INVESTIGATED BY ATOMIC FORCE MICROSCOPY

2004 ◽  
Vol 11 (01) ◽  
pp. 71-75
Author(s):  
Y. L. GENG ◽  
D. XU ◽  
D. L. SUN ◽  
X. Q. WANG ◽  
G. H. ZHANG ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Stress Field ◽  
Single Crystals ◽  
Liquid Flow ◽  
Two Dimensional ◽  
Characteristic Structure ◽  
Force Microscopy ◽  
Atomic Force ◽  
Dislocation Sources ◽  
Extra Stress

Growth hillocks on the {100} faces of L-arginine phosphate monohydrate (LAP) single crystals grown at 25°C and at a supersaturation of 0.32 have been discussed. The typical dislocation growth hillocks are lopsided and elongate along the b direction. The dislocation sources are probably caused by the extra stress field which is introduced by the hollow cavities distributing on the steps and hillocks generated by the two-dimensional nucleus. The elongated shape is due to the characteristic structure of the LAP crystal. Apart from that, the formation of the lopsided growth hillocks is explained by the liquid flow theory.

scholarly journals Probing the Enzymatic Activity of Individual Biocatalytic fd-Viral Particles by Electrochemical-Atomic Force Microscopy

ACS Catalysis ◽  
2020 ◽  
Vol 10 (14) ◽  
pp. 7843-7856
Author(s):  
Telmo O. Paiva ◽  
Kristian Torbensen ◽  
Anisha N. Patel ◽  
Agnès Anne ◽  
Arnaud Chovin ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Enzymatic Activity ◽  
Force Microscopy ◽  
Atomic Force ◽  
Viral Particles

Surface morphology of {100} faces ofL-arginine phosphate monohydrate single crystals investigated by atomic force microscopy

2005 ◽  
Vol 38 (4) ◽  
pp. 657-660 ◽  
Author(s):  
Y. L. Geng ◽  
D. Xu ◽  
X. Q. Wang ◽  
G. H. Zhang ◽  
G. W. Yu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Atomic Force Microscopy ◽  
Surface Morphology ◽  
Single Crystals ◽  
Liquid Flow ◽  
Growth Conditions ◽  
Mother Solution ◽  
Two Dimensional ◽  
Force Microscopy ◽  
Atomic Force

Surface morphology of {100} faces of LAP crystals was investigated by atomic force microscopy (AFM). Both the steps and the two-dimensional nuclei elongate along thebdirection, which is determined by the crystal structure. Fluctuations in the growth conditions could result in the formation of protuberances on the step fronts. Tree-like growth belts are initially observed on LAP crystals. It is assumed that the formation is caused by uneven liquid flow of the mother solution.

scholarly journals AFM and FTIR Investigation of the Effect of Water Flow on Horseradish Peroxidase

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 306
Author(s):  
Yuri D. Ivanov ◽  
Tatyana O. Pleshakova ◽  
Ivan D. Shumov ◽  
Andrey F. Kozlov ◽  
Anastasia A. Valueva ◽  
...  
Keyword(s):  
Horseradish Peroxidase ◽  
Enzymatic Activity ◽  
Substrate Surface ◽  
Solid Substrate ◽  
Attenuated Total Reflection ◽  
Flow Section ◽  
Force Microscopy ◽  
Atomic Force ◽  
Influence Of Water ◽  
Actual Direction

Atomic force microscopy (AFM)-based fishing is a promising method for the detection of low-abundant proteins. This method is based on the capturing of the target proteins from the analyzed solution onto a solid substrate, with subsequent counting of the captured protein molecules on the substrate surface by AFM. Protein adsorption onto the substrate surface represents one of the key factors determining the capturing efficiency. Accordingly, studying the factors influencing the protein adsorbability onto the substrate surface represents an actual direction in biomedical research. Herein, the influence of water motion in a flow-based system on the protein adsorbability and on its enzymatic activity has been studied with an example of horseradish peroxidase (HRP) enzyme by AFM, attenuated total reflection Fourier-transform infrared spectroscopy (ATR-FTIR) and conventional spectrophotometry. In the experiments, HRP solution was incubated in a setup modeling the flow section of a biosensor communication. The measuring cell with the protein solution was placed near a coiled silicone pipe, through which water was pumped. The adsorbability of the protein onto the surface of the mica substrate has been studied by AFM. It has been demonstrated that incubation of the HRP solution near the coiled silicone pipe with flowing water leads to an increase in its adsorbability onto mica. This is accompanied by a change in the enzyme’s secondary structure, as has been revealed by ATR-FTIR. At the same time, its enzymatic activity remains unchanged. The results reported herein can be useful in the development of models describing the influence of liquid flow on the properties of enzymes and other proteins. The latter is particularly important for the development of biosensors for biomedical applications—particularly for serological analysis, which is intended for the early diagnosis of various types of cancer and infectious diseases. Our results should also be taken into account in studies of the effects of protein aggregation on hemodynamics, which plays a key role in human body functioning.

Monitoring the HIV-1 integrase enzymatic activity using atomic force microscopy in a 2LTR system

2013 ◽  
Vol 49 (30) ◽  
pp. 3113 ◽  
Author(s):  
Shlomit Guy ◽  
Dvir Rotem ◽  
Zvi Hayouka ◽  
Ronen Gabizon ◽  
Aviad Levin ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Enzymatic Activity ◽  
Force Microscopy ◽  
Atomic Force ◽  
Hiv 1
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