Comparison of the Results of SPR Analysis of Antigen-antibody Interactions Performed Using Optical Biosensors Biacore X-100 (Cytiva, USA) and MI-S200D (Inter-Bio, China)
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| Název: | Comparison of the Results of SPR Analysis of Antigen-antibody Interactions Performed Using Optical Biosensors Biacore X-100 (Cytiva, USA) and MI-S200D (Inter-Bio, China) |
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| Autoři: | Gnedenko, O.V., Mezentsev, Y.V., Yablokov, E.O., Kaluzhskiy, L.A., Ershov, P.V., Gilep, A.A., Ivanov, A.S. |
| Zdroj: | Biomedical Chemistry: Research and Methods; Vol. 7 No. 4 (2024); e00246 Biomedical Chemistry: Research and Methods; Том 7 № 4 (2024); e00246 |
| Informace o vydavateli: | Institute of Biochemistry, 2024. |
| Rok vydání: | 2024 |
| Témata: | равновесная константа диссоциации (Kd), константы скорости образования и распада комплекса (kon, koff), взаимодействие антиген-антитело, оптические биосенсоры, поверхностный плазмонный резонанс (SPR), equilibrium dissociation constant (Kd), rate constants of assoсiation and dissociation of the complex (kon, koff), antigen-antibody interaction, optical biosensors, surface plasmon resonance (SPR) |
| Popis: | Limited availability of Western scientific equipment, explains a growing need to switch to using scientific instruments made in China. This is especially true in the case of optical biosensors operating on the surface plasmon resonance (SPR) effect. However, comparability of experimental data obtained using Western and Chinese biosensors has not been investigated yet. In this work we have comparedresults of SPR analysis of the kinetics and affinity of interaction of IgG2a and IgG1 antibodies with protein A. Two biosensos Biacore X-100 (Cytiva, USA) and MI-S200D (Inter-Bio, China) have been used. It was shown that the values of the association rate constants obtained on both devices for two antibodies were close within one order of magnitude. For IgG1 antibodies, the dissociation rate constants were almost identical. Both devices provide high-quality data that are well described by a simple 1:1 model (Langmuir binding). |
| Druh dokumentu: | Article |
| Popis souboru: | application/pdf; text/html |
| Jazyk: | English |
| ISSN: | 2618-7531 |
| DOI: | 10.18097/bmcrm00246 |
| Přístupová URL adresa: | http://www.bmc-rm.org/index.php/BMCRM/article/view/246 |
| Přístupové číslo: | edsair.doi.dedup.....efaced4f088d0a7c4f85e976d55f1c2c |
| Databáze: | OpenAIRE |
Nájsť tento článok vo Web of Science | Abstrakt: | Limited availability of Western scientific equipment, explains a growing need to switch to using scientific instruments made in China. This is especially true in the case of optical biosensors operating on the surface plasmon resonance (SPR) effect. However, comparability of experimental data obtained using Western and Chinese biosensors has not been investigated yet. In this work we have comparedresults of SPR analysis of the kinetics and affinity of interaction of IgG2a and IgG1 antibodies with protein A. Two biosensos Biacore X-100 (Cytiva, USA) and MI-S200D (Inter-Bio, China) have been used. It was shown that the values of the association rate constants obtained on both devices for two antibodies were close within one order of magnitude. For IgG1 antibodies, the dissociation rate constants were almost identical. Both devices provide high-quality data that are well described by a simple 1:1 model (Langmuir binding). |
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| ISSN: | 26187531 |
| DOI: | 10.18097/bmcrm00246 |