Detection of hepatitis C virus core protein in serum by atomic force microscopy combined with&amp;nbsp;mass spectrometry

Ivanov, Yuri D.; Kaysheva, Anna L.; Frantsuzov, P. A.; Pleshakova, Tatyana O.; Krohin, N. V.; Izotov, Alexander; Shumov, Ivan D.; Учайкин, В. Ф.; Konev, V. A.; Ziborov, Vadim S.; Archakov, Alexander I.

doi:10.2147/ijn.s71776

Cited by 13 publications

(2 citation statements)

References 22 publications

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“…The first way suggests the digestion of the sample immediately on the surface of the membrane carrier. Another way supposes digestion of the sample following preliminary elution from the surface of DBS wherein the procedure of samples preparation addressed for the mass spectrometry analysis is being typical and described repeatedly in numerous publications including our authored papers [24][25][26].…”

Section: Resultsmentioning

confidence: 99%

Stability of Plasma Protein Composition in Dried Blood Spot during Storage

et al. 2020

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Dried blood spot (DBS) technology has become a promising utility for the transportation and storage of biological fluids aimed for the subsequent clinical analysis. The basis of the DBS method is the adsorption of the components of a biological sample onto the surface of a membrane carrier, followed by drying. After drying, the molecular components of the biosample (nucleic acids, proteins, and metabolites) can be analyzed using modern omics, immunological, or genomic methods. In this work, we investigated the safety of proteins on a membrane carrier by tryptic components over time and at different temperatures (+4, 0, 25 °C) and storage (0, 7, 14, and 35 days). It was shown that the choice of a protocol for preliminary sample preparation for subsequent analytical molecular measurements affects the quality of the experimental results. The protocol for preliminary preparation of a biosample directly in a membrane carrier is preferable compared to the protocol with an additional stage of elution of molecular components before the sample preparation procedures. It was revealed that the composition of biosamples remains stable at a temperature of −20 and +4 °C for 35 days of storage, and at +25 °C for 14 days.

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Section: Resultsmentioning

confidence: 99%

Stability of Plasma Protein Composition in Dried Blood Spot during Storage

et al. 2020

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“…Atomic force microscopy (AFM) and mass spectrometry (MS) were employed in order to confirm the efficiency of the technique used for the sensitization of the NRs. Such an approach was shown to be an efficient tool in studying antibody-antigen [38] and aptamer-antigen [39,40] complexes on the surface of solid substrates sensitized with molecular probes. Since immobilized aptamers are barely distinguishable on the AFM substrate surface, the efficiency of the sensitization of the substrate surface with aptamers is estimated after the formation of aptamer-antigen complexes on it [39].…”

Section: Introductionmentioning

confidence: 99%

Aptamer-Sensitized Nanoribbon Biosensor for Ovarian Cancer Marker Detection in Plasma

et al. 2021

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The detection of CA 125 protein in buffer solution with a silicon-on-insulator (SOI)-based nanoribbon (NR) biosensor was experimentally demonstrated. In the biosensor, sensor chips, bearing an array of 12 nanoribbons (NRs) with n-type conductance, were employed. In the course of the analysis with the NR biosensor, the target protein was biospecifically captured onto the surface of the NRs, which was sensitized with covalently immobilized aptamers against CA 125. Atomic force microscopy (AFM) and mass spectrometry (MS) were employed in order to confirm the formation of the probe–target complexes on the NR surface. Via AFM and MS, the formation of aptamer–antigen complexes on the surface of SOI substrates with covalently immobilized aptamers against CA 125 was revealed, thus confirming the efficient immobilization of the aptamers onto the SOI surface. The biosensor signal, resulting from the biospecific interaction between CA 125 and the NR-immobilized aptamer probes, was shown to increase with an increase in the target protein concentration. The minimum detectable CA 125 concentration was as low as 1.5 × 10−17 M. Moreover, with the biosensor proposed herein, the detection of CA 125 in the plasma of ovarian cancer patients was demonstrated.

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Highly sensitive protein detection by biospecific AFM‐based fishing with pulsed electrical stimulation

et al. 2017

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We report here the highly sensitive detection of protein in solution at concentrations from 10 –15 to 10 –18 m using the combination of atomic force microscopy ( AFM ) and mass spectrometry. Biospecific detection of biotinylated bovine serum albumin was carried out by fishing out the protein onto the surface of AFM chips with immobilized avidin, which determined the specificity of the analysis. Electrical stimulation was applied to enhance the fishing efficiency. A high sensitivity of detection was achieved by application of nanosecond electric pulses to highly oriented pyrolytic graphite placed under the AFM chip. A peristaltic pump‐based flow system, which is widely used in routine bioanalytical assays, was employed throughout the analysis. These results hold promise for the development of highly sensitive protein detection methods using nanosensor devices.

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Detection of hepatitis C virus core protein in serum by atomic force microscopy combined with mass spectrometry

Cited by 13 publications

References 22 publications

Stability of Plasma Protein Composition in Dried Blood Spot during Storage

Stability of Plasma Protein Composition in Dried Blood Spot during Storage

Aptamer-Sensitized Nanoribbon Biosensor for Ovarian Cancer Marker Detection in Plasma

Highly sensitive protein detection by biospecific AFM‐based fishing with pulsed electrical stimulation

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