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1.
Sci Rep ; 14(1): 23838, 2024 10 11.
Artigo em Inglês | MEDLINE | ID: mdl-39394398

RESUMO

Myocardial infarction is a major cause of morbidity and mortality worldwide. Metabolomic investigations may be useful for understanding the pathogenesis of ST-segment elevation myocardial infarction (STEMI). STEMI patients were comprehensively examined via targeted metabolomic profiling, machine learning and weighted correlation network analysis. A total of 195 subjects, including 68 STEMI patients, 84 patients with stable angina pectoris (SAP) and 43 non-CVD patients, were enrolled in the study. Metabolomic profiling involving the quantitative analysis of 87 endogenous metabolites in plasma was conducted. This study is the first to perform targeted metabolomic profiling in patients with STEMI. We identified 36 significantly altered metabolites in STEMI patients. Increased levels of four amino acids, eight acylcarnitines, six metabolites of the NO-urea cycle and neurotransmitters, and three intermediates of tryptophan metabolism were detected. The following metabolites exhibited decreased levels: six amino acids, three acylcarnitines, three components of the NO-urea cycle and neurotransmitters, and three intermediates of tryptophan metabolism. We found that the significant changes in tryptophan metabolism observed in STEMI patients-the increase in anthranilic acid and tryptophol and decrease in xanthurenic acid and 3-OH-kynurenine-may play important roles in STEMI pathogenesis. On the basis of the differences in the constructed weighted correlation networks, new significant metabolite ratios were identified. Among the 22 significantly altered metabolite ratios identified, 13 were between STEMI patients and non-CVD patients, and 17 were between STEMI patients and SAP patients. Seven of these ratios were common to both comparisons (STEMI patients vs. non-CVD patients and STEMI patients vs. SAP patients). Additionally, two ratios were consistently observed among the STEMI, SAP and non-CVD groups (anthranilic acid: aspartic acid and GSG (glutamine: serine + glycine)). These findings provide new insight into the diagnosis and pathogenesis of STEMI.


Assuntos
Metabolômica , Infarto do Miocárdio com Supradesnível do Segmento ST , Humanos , Masculino , Feminino , Infarto do Miocárdio com Supradesnível do Segmento ST/metabolismo , Infarto do Miocárdio com Supradesnível do Segmento ST/sangue , Metabolômica/métodos , Pessoa de Meia-Idade , Idoso , Metaboloma , Triptofano/metabolismo , Triptofano/sangue , Aminoácidos/metabolismo , Aminoácidos/sangue , Biomarcadores/sangue
2.
Biomed Khim ; 70(5): 263-272, 2024 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-39324192

RESUMO

Eighty years ago, the Institute of Biomedical Chemistry (IBMC) initially known as the Institute of Biological and Medical Chemistry of the Academy of Sciences of the USSR was founded. During the first decades significant studies were performed; they not only contributed to a deeper understanding of biochemical processes in the living organisms, but also laid the foundation for further development of these fields. The main directions of IBMC were focused on studies of structures of enzymes (primarily various proteases), their substrates and inhibitors, the role of enzymes of carbohydrate metabolism in the development of pathologies, study of the mechanisms of hydrolytic and oxidative-hydrolytic transformation of organic compounds, studies of connective tissue proteins, including collagens, study of amino acid metabolism. It is difficult to find papers from that period in current online literature databases, so this review will help to understand the value of studies performed at IBMC during the first 40 years after its organization, as well as their impact on modern research.


Assuntos
Proteínas , Animais , Humanos , Academias e Institutos/história , Metabolismo dos Carboidratos , História do Século XX , História do Século XXI , Proteínas/química , Proteínas/metabolismo
3.
Biomed Khim ; 70(5): 273-286, 2024 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-39324193

RESUMO

The review considers the possibility of using atomic force microscopy (AFM) as a basic method for protein detection in solutions with low protein concentrations. The demand for new bioanalytical approaches is determined by the problem of insufficient sensitivity of systems used in routine practice for protein detection. Special attention is paid to demonstration of the use in bioanalysis of a combination of AFM and fishing methods as an approach of concentrating biomolecules from a large volume of the analyzed solution on a small surface area.


Assuntos
Microscopia de Força Atômica , Proteínas , Microscopia de Força Atômica/métodos , Proteínas/análise , Proteínas/química , Humanos , Animais , Soluções
4.
Biomed Khim ; 70(5): 304-314, 2024 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-39324195

RESUMO

The review considers modern achievements and prospects of using nanowire biosensors, principles of their operation, methods of fabrication, and the influence of the Debye effect, which plays a key role in improving the biosensor characteristics. Special attention is paid to the practical application of such biosensors for the detection of a variety of biomolecules, demonstrating their capabilities and potential in the detection of a wide range of biomarkers of various diseases. Nanowire biosensors also show excellent results in such areas as early disease diagnostics, patient health monitoring, and personalized medicine due to their high sensitivity and specificity. Taking into consideration their high efficiency and diverse applications, nanowire-based biosensors demonstrate significant promise for commercialization and widespread application in medicine and related fields, making them an important area for future research and development.


Assuntos
Técnicas Biossensoriais , Nanofios , Técnicas Biossensoriais/instrumentação , Técnicas Biossensoriais/métodos , Nanofios/química , Humanos , Biomarcadores/análise , Medicina de Precisão/métodos , Medicina de Precisão/instrumentação
5.
Sci Rep ; 14(1): 2651, 2024 02 01.
Artigo em Inglês | MEDLINE | ID: mdl-38302683

RESUMO

Cardiovascular disease (CVD) represents one of the main causes of mortality worldwide and nearly a half of it is related to ischemic heart disease (IHD). The article represents a comprehensive study on the diagnostics of IHD through the targeted metabolomic profiling and machine learning techniques. A total of 112 subjects were enrolled in the study, consisting of 76 IHD patients and 36 non-CVD subjects. Metabolomic profiling was conducted, involving the quantitative analysis of 87 endogenous metabolites in plasma. A novel regression method of age-adjustment correction of metabolomics data was developed. We identified 36 significantly changed metabolites which included increased cystathionine and dimethylglycine and the decreased ADMA and arginine. Tryptophan catabolism pathways showed significant alterations with increased levels of serotonin, intermediates of the kynurenine pathway and decreased intermediates of indole pathway. Amino acid profiles indicated elevated branched-chain amino acids and increased amino acid ratios. Short-chain acylcarnitines were reduced, while long-chain acylcarnitines were elevated. Based on these metabolites data, machine learning algorithms: logistic regression, support vector machine, decision trees, random forest, and gradient boosting, were used for IHD diagnostic models. Random forest demonstrated the highest accuracy with an AUC of 0.98. The metabolites Norepinephrine; Xanthurenic acid; Anthranilic acid; Serotonin; C6-DC; C14-OH; C16; C16-OH; GSG; Phenylalanine and Methionine were found to be significant and may serve as a novel preliminary panel for IHD diagnostics. Further studies are needed to confirm these findings.


Assuntos
Doenças Cardiovasculares , Isquemia Miocárdica , Humanos , Serotonina , Aminoácidos , Metabolômica/métodos , Aminoácidos de Cadeia Ramificada/metabolismo , Isquemia Miocárdica/complicações , Doenças Cardiovasculares/etiologia
6.
Bull Exp Biol Med ; 167(1): 91-96, 2019 May.
Artigo em Inglês | MEDLINE | ID: mdl-31177467

RESUMO

Comparative mass spectrometric analysis of protein composition was carried out in 36 blood plasma specimens from patients with renal cell carcinoma and 20 specimens from donors. Analysis of protein composition of plasma specimens devoid of the major protein fractions showed a 20-50% higher level of protein identifications in patient' specimens. Specimens of the control and experimental series were similar by protein composition, 70-80% identifications in experimental and control series coinciding. High similarity of biological processes with participation of the proteins identified in both series was observed. The greater part of proteins in both series were located extracellularly and were exosomal (specimens from renal cancer patients) or vesicular (specimens from healthy volunteers).


Assuntos
Proteínas Sanguíneas/análise , Carcinoma de Células Renais/sangue , Neoplasias Renais/sangue , Proteoma/análise , Biomarcadores Tumorais/sangue , Cromatografia Líquida , Feminino , Humanos , Masculino , Proteômica/métodos , Espectrometria de Massas em Tandem
7.
J Virol Methods ; 251: 99-105, 2018 01.
Artigo em Inglês | MEDLINE | ID: mdl-29042217

RESUMO

In the present study, the possibility of hepatitis C virus core antigen (HCVcoreAg) detection in buffer solution, using atomic force microscope chip (AFM-chip) with immobilized aptamers, has been demonstrated. The target protein was detected in 1mL of solution at concentrations from 10-10М to 10-13М. The registration of aptamer/antigen complexes on the chip surface was carried out by atomic force microscopy (AFM). The further mass-spectrometric (MS) identification of AFM-registered objects on the chip surface allowed reliable identification of HCVcoreAg target protein in the complexes. Aptamers, which were designed for therapeutic purposes, have been shown to be effective in HCVcoreAg detection as probe molecules.


Assuntos
Aptâmeros de Nucleotídeos/metabolismo , Microscopia de Força Atômica/métodos , Proteínas do Core Viral/análise
8.
Patol Fiziol Eksp Ter ; 61(2): 101-7, 2017.
Artigo em Russo | MEDLINE | ID: mdl-29215851

RESUMO

The purpose of the research consisted in detection of fluctuation of brightness temperature (TSHF) of water in the area of the temperature Т = 42°Ð¡ (that is critical for human) during its evaporation by SHF radiometry. Methods: Monitoring of the changes in brightness temperature of water in superhigh frequency (SHF) range (3.8-4.2 GHz) near the phase transition temperature of water Т = 42°Ð¡ during its evaporation in the cone dielectric cell. The brightness temperature measurements were carried out using radiometer. Results: Fluctuation with maximum of brightness temperature was detected in 3.8-4.2 GHz frequency range near at the temperature of water Т = 42°Ð¡. It was characteristic for these TSHF fluctuations that brightness temperature rise time in this range of frequencies in ~4°Ð¡ temperature range with 0.05-15°Ð¡/min gradient and a sharp decrease during 10 s connected with measuring vapor conditions. Then nonintensive fluctuation series was observed. At that, the environment temperature remained constant. Conclusion: The significant increasing in brightness temperature of water during its evaporation in SHF range near the temperature of Т ~42°Ð¡ were detected. It was shown that for water, ТSHF pull with the amplitude DТSHF ~4°C are observed. At the same time, thermodynamic temperature virtually does not change. The observed effects can be used in the development of the systems for diadnostics of pathologies in human and analytical system.


Assuntos
Temperatura Alta , Micro-Ondas , Água/química
9.
J Mol Neurosci ; 62(3-4): 420-429, 2017 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-28730336

RESUMO

According to WHO data, about 67 million people worldwide are affected by autism, and this number grows by 14% annually. Among the possible causes of autism are genetic modifications, organic lesions of the central nervous system, metabolic disorders, influence of viral and bacterial infections, chemical influence to the mother's body during pregnancy, etc. The conducted research shows that research papers published until today do not name any potential protein markers that meet the requirements of the basic parameters for evaluating the efficiency of disease diagnostics, in particular high sensitivity, specificity, and accuracy. Conducting proteomic research on a big scale in order to detect serologic markers of protein nature associated with development of autism spectrum disorders seems to be highly relevant.


Assuntos
Transtorno do Espectro Autista/sangue , Transtorno do Espectro Autista/genética , Autoanticorpos/sangue , Biomarcadores/sangue , Citocinas/sangue , Humanos , Peptídeos/sangue , Serotonina/sangue
10.
Biomed Khim ; 62(4): 439-46, 2016 May.
Artigo em Russo | MEDLINE | ID: mdl-27562998

RESUMO

A combination of (atomic force microscopy)-based fishing (AFM-fishing) and mass spectrometry allows to capture protein molecules from solutions, concentrate and visualize them on an atomically flat surface of the AFM chip and identify by subsequent mass spectrometric analysis. In order to increase the AFM-fishing efficiency we have applied pulsed voltage with the rise time of the front of about 1 ns to the AFM chip. The AFM-chip was made using a conductive material, highly oriented pyrolytic graphite (HOPG). The increased efficiency of AFM-fishing has been demonstrated using detection of cytochrome b5 protein. Selection of the stimulating pulse with a rise time of 1 ns, corresponding to the GHz frequency range, by the effect of intrinsic emission from water observed in this frequency range during water injection into the cell.


Assuntos
Citocromos b5/química , Espectrometria de Massas/métodos , Microscopia de Força Atômica/métodos , Proteoma/química , Campos Eletromagnéticos , Humanos , Microscopia de Força Atômica/instrumentação
11.
Patol Fiziol Eksp Ter ; 60(4): 174-7, 2016.
Artigo em Inglês | MEDLINE | ID: mdl-29244941

RESUMO

The purpose: The purpose of this research consisted in monitoring of brightness temperature of the suspension of follicular thyroid carcinoma cells during the necrosis of these cells in superhigh frequency (SHF) range. Methods: The monitoring of the change in the ratio between brightness temperatures TSHF and TIR values during the necrosis of these cells. The object of study was follicular thyroid carcinoma cells suspension prepared with use of Versene solution and 0.25% trypsin solution. The cells were precipitated by centrifugation and re-suspended in culture medium. The measurements of brightness temperatures were carried out with use of radiothermoimeter. SHF range was 3.4-4.2 GHz, and infrared (IR) range was 8-13 mm. The temperature of the suspension was maintained at 37.5°Ð¡. Results: It was found that upon the necrosis in the suspension of cells, an increase in brightness temperature in 3.4-4.2 GHz range (SHF range) occurs, while brightness temperature of the medium in the IR range does not change. Conclusion: The monitoring of necrosis of follicular thyroid carcinoma cells was carried out by SHF-radiothermometry. It was shown that during the necrosis the change of non-equilibrium state of cell medium occurs, that results in the change in the ratio between TSHF and TIR. During the necrosis, the brightness temperature in SHF range (TSHF) increases.


Assuntos
Adenocarcinoma Folicular/metabolismo , Adenocarcinoma Folicular/patologia , Ondas de Rádio , Termometria/métodos , Neoplasias da Glândula Tireoide/metabolismo , Neoplasias da Glândula Tireoide/patologia , Linhagem Celular Tumoral , Humanos
12.
Biochem Biophys Rep ; 5: 285-289, 2016 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-28955835

RESUMO

Microwave radiation at 3.4-4.2 GHz frequency of the cytochrome P450 CYP102 A1 (BM3) solution was registered during the lauric acid hydroxylation reaction. The microwave radiation generation was shown to occur following the addition of electron donor NADPH to a system containing an enzyme and a substrate. The radiation occurs for the enzyme solutions with enzyme concentrations of 10-8 and 10-9 Ðœ. The microwave radiation effect elicited by the aqueous enzyme solution was observed for the first time. The results obtained can be used to elaborate a new approach to enzyme systems research, including studying of the mechanism of interaction of a functioning enzyme system with microenvironment.

13.
Patol Fiziol Eksp Ter ; 60(1): 94-8, 2016.
Artigo em Russo | MEDLINE | ID: mdl-29215256

RESUMO

A method for detection of cancer-associated protein D-NFATc1 in serum using nanowire (NW) biosensor based on field-effect nanotransistor is developed. Field-effect nanotransistor was fabricated on the basis of «silicon-on-insulator¼ structures. For the biospecific detection of target protein, the NW surface was modified with aptamers against the target protein. Using the 3 um-NW enabled to obtain stable source-drain characteristics and to register D-NFATc1 in serum at concentration of 2.5 x 1014 M in the mode of drain-source current vs. gate voltage characteristics measurements. Data collection in the mode of drain-source current vs. gate voltage characteristics measurements was carried out with the use of high-speed data collection system running TURBO NBS software.


Assuntos
Técnicas Biossensoriais , Fatores de Transcrição NFATC/sangue , Nanofios , Proteínas de Neoplasias/sangue , Software , Transistores Eletrônicos , Técnicas Biossensoriais/instrumentação , Técnicas Biossensoriais/métodos , Humanos , Sensibilidade e Especificidade
14.
Biomed Khim ; 61(4): 462-7, 2015.
Artigo em Russo | MEDLINE | ID: mdl-26350736

RESUMO

The nanowire (NW) detection is one of fast-acting and high-sensitive methods allowing to reveal potentially relevant protein molecules. A NW biosensor based on the silicon-on-insulator (SOI)-structures was used for biospecific label-free detection of NFAT 1 (D-NFAT 1) oncomarker in real time. For this purpose, SOI-nanowires (NWs) were modified with aptamers against NFAT 1 used as molecular probes. It was shown that using this biosensor it is possible to reach the sensitivity of ~10(-15) M. This sensitivity was comparable with that of the NW biosensor with immobilized antibodies used as macromolecular probes. The results demonstrate promising approaches used to form the sensor elements for high-sensitive disease diagnostics.


Assuntos
Aptâmeros de Nucleotídeos/química , Técnicas Biossensoriais/instrumentação , Fatores de Transcrição NFATC/análise , Nanofios/química , Proteínas de Neoplasias/análise , Anticorpos Monoclonais/química , Aptâmeros de Nucleotídeos/síntese química , Técnicas Biossensoriais/economia , Técnicas Eletroquímicas , Humanos , Limite de Detecção , Dióxido de Silício/química , Soluções , Succinimidas/química
15.
Biomed Khim ; 61(3): 363-72, 2015.
Artigo em Russo | MEDLINE | ID: mdl-26215414

RESUMO

A method of atomic force microscopy-based fishing (AFM fishing) has been developed for protein detection in the analyte solution using a chip with an immobilized aptamer. This method is based on the biospecific fishing of a target protein from a bulk solution onto the small AFM chip area with the immobilized aptamer to this protein used as the molecular probe. Such aptamer-based approach allows to increase an AFM image contrast compared to the antibody-based approach. Mass spectrometry analysis used after the biospecific fishing to identify the target protein on the AFM chip has proved complex formation. Use of the AFM chip with the immobilized aptamer avoids interference of the antibody and target protein peaks in a mass spectrum.


Assuntos
Aptâmeros de Nucleotídeos/química , Proteína gp120 do Envelope de HIV/análise , Ácidos Nucleicos Imobilizados/química , Microscopia de Força Atômica/métodos , Anticorpos Imobilizados/química , Aptâmeros de Nucleotídeos/análise , Proteína gp120 do Envelope de HIV/imunologia , Microscopia de Força Atômica/instrumentação , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos
16.
Biomed Khim ; 61(2): 239-53, 2015.
Artigo em Russo | MEDLINE | ID: mdl-25978390

RESUMO

Achievement of the concentration detection limit for proteins at the level of the reverse Avogadro number determines the modern development of proteomics. In this review, the possibility of approximating the reverse Avogadro number by using nanotechnological methods (AFM-based fishing with mechanical and electrical stimulation, nanowire detectors, and other methods) are discussed. The ability of AFM to detect, count, visualize and characterize physico-chemical properties of proteins at concentrations up to 10(-17)-10(-18) M is demonstrated. The combination of AFM-fishing with mass-spectrometry allows the identification of proteins not only in pure solutions, but also in multi-component biological fluids (serum). The possibilities to improve the biospecific fishing efficiency by use of SOMAmers in both AFM and nanowire systems are discussed. The paper also provides criteria for evaluation of the sensitivity of fishing-based detection systems. The fishing efficiency depending on the detection system parameters is estimated. The practical implementation of protein fishing depending on the ratio of the sample solution volume and the surface of the detection system is discussed. The advantages and disadvantages of today's promising nanotechnological protein detection methods implemented on the basis of these schemes.


Assuntos
Microscopia de Força Atômica/métodos , Proteínas/análise , Animais , Técnicas Biossensoriais/métodos , Técnicas Eletroquímicas/instrumentação , Técnicas Eletroquímicas/métodos , Ensaio de Imunoadsorção Enzimática , Humanos , Limite de Detecção , Espectrometria de Massas , Microscopia de Força Atômica/instrumentação , Técnicas de Sonda Molecular , Nanotecnologia/métodos , Nanofios , Proteínas/metabolismo , Ressonância de Plasmônio de Superfície/métodos
17.
Biofizika ; 60(1): 80-7, 2015.
Artigo em Russo | MEDLINE | ID: mdl-25868344

RESUMO

The change in temperature is one of the factors affecting the activity of enzymes. In this work thermal denaturation and aggregation of cytochrome P450 BM3 were studied by atomic force microscopy. To determine specific temperature transitions the fluorescence analysis was used. In the low melting temperature range, 10-33 degrees C, a decrease in the fluorescence intensity of aromatic residues was observed with an increase in the fluorescence intensity of flavin groups. Protein melting in this range indicated three narrow S-shaped cooperative transitions at temperatures 16, 22 and 29 degrees C. Atomic force microscopy analysis in this temperature range showed that the shape of BM3 molecules remained globular in the form of compact objects (heights h < 7 nm, lateral dimensions d < 50 nm), but protein oligomeric state changed. The first two transitions were accompanied by a decrease in the degree of oligomerization and the third one was accompanied by its increase.


Assuntos
Sistema Enzimático do Citocromo P-450/química , Sistema Enzimático do Citocromo P-450/ultraestrutura , Temperatura Alta , Microscopia de Força Atômica , Multimerização Proteica , Estrutura Terciária de Proteína
18.
Biomed Khim ; 60(1): 28-50, 2014.
Artigo em Russo | MEDLINE | ID: mdl-24749246

RESUMO

The atomic-force microscopy-based method of irreversible chemical AFM-fishing (AFM-IF(Ch)) has been developed for the detection of proteins at ultra-low concentrations in solution. Using this method, a very low concentration of horseradish peroxidase (HRP) protein (10(-17) M) was detected in solution. A theoretical model that allows the description of obtained experimental data, is proposed. This model takes into consideration both the transport of the protein from the bulk solution onto the AFM-chip surface and its irreversible binding to the activated area.


Assuntos
Avidina/isolamento & purificação , Proteínas do Ovo/isolamento & purificação , Peroxidase do Rábano Silvestre/isolamento & purificação , Microscopia de Força Atômica/métodos , Simulação por Computador , Cinética , Dispositivos Lab-On-A-Chip , Microscopia de Força Atômica/instrumentação , Modelos Químicos , Ligação Proteica , Soluções
19.
Biofizika ; 56(5): 939-44, 2011.
Artigo em Russo | MEDLINE | ID: mdl-22117449

RESUMO

An approach to measure the activity of single oligomers of the heme-containing enzyme the cytochrome P450 CYP102A1 (CYP102A1) by atomic force microscopy (AFM) has been developed. It was found that the amplitude of fluctuations of the height of single CYP102A1 molecules performing the catalytic cycle is twice as great as the amplitude of fluctuations of the height of the same enzymes in the inactive state. It was shown that the amplitude of height fluctuations of a CYP102A1 protein globule depends on temperature, the maximum of this dependence being observed at 22 degrees C. The activity of a single CYP102A1 molecule in the unit amplitude of height fluctuations of a protein globule reduced to the unit time was 5+/-2 Ac. The elasticity of a single protein molecule was measured from the deformation of this molecule by the action of an AFM probe. The use of AFM probes of different geometry made i t possible t o determine t he integral andlocal Young's modulus for the monomers of the protein putidaredoxin reductase from the cytochrome P450 CYP101 (P450cam)-containing monooxigenase system, which were 37+/-117 and 1+/-3 MPa, respectively.


Assuntos
Proteínas de Bactérias/ultraestrutura , Sistema Enzimático do Citocromo P-450/ultraestrutura , Complexos Multiproteicos/ultraestrutura , NADPH-Ferri-Hemoproteína Redutase/ultraestrutura , Proteínas de Bactérias/química , Sistema Enzimático do Citocromo P-450/química , Hidroxilação , Microscopia de Força Atômica/métodos , Complexos Multiproteicos/química , NADPH-Ferri-Hemoproteína Redutase/química
20.
Biomed Khim ; 56(1): 26-39, 2010.
Artigo em Russo | MEDLINE | ID: mdl-21328909

RESUMO

Possibility of detection and identification of hepatitis C viral particles with mass spectrometry (MS) in combination with atomic force microscopy (AFM) had been investigated. AFM/MS approach is based on two technologies: (1) AFM-biospecific fishing that allows to detect, concentrate from solution and to count protein complexes on a surface of AFM-nanochip; (2) mass spectrometric identification of these complexes. AFM-biospecific fishing of HCVcoreAg from solution was carried onto surface of AFM-nanochips with immobilized anti-HCVcoreAg. It was shown that HCVcoreAg/anti-HCVcore(im) complexes were formed onto AFM-nanochips in quantity sufficient for mass spectrometric identification. Thus, AFM/MS approach allows to identify fragments of hepatitis C virus fished onto a surface of AFM-nanochip from serum.


Assuntos
Hepacivirus , Vírion , Sequência de Aminoácidos , Anticorpos Monoclonais , Hepacivirus/imunologia , Hepatite C/sangue , Antígenos da Hepatite C/análise , Antígenos da Hepatite C/imunologia , Humanos , Dispositivos Lab-On-A-Chip , Microscopia de Força Atômica , Dados de Sequência Molecular , Proteínas Recombinantes/análise , Proteínas Recombinantes/imunologia , Espectrometria de Massas por Ionização por Electrospray , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz , Espectrometria de Massas em Tandem , Vírion/imunologia , Virologia/métodos
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