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Label-Free and Real-Time Monitor of Binding and Dissociation Processes between Protein A and Swine IgG by Oblique-Incidence Reflectivity Difference Method |
| HE Li-Ping1, LIU Shuang1, DAI Jun1, WU Lin2, LIU Guo-Zhen3, WEI Han-Fu3, LU Hui-Bin1**, JIN Kui-Juan1, YANG Guo-Zhen1 |
1Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190
2Key Laboratory of Genome Sciences and Information, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100101
3Beijing Protein Innovation Co. Ltd., Beijing 101318
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| Cite this article: |
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HE Li-Ping, LIU Shuang, DAI Jun et al 2015 Chin. Phys. Lett. 32 020703 |
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Abstract Life science has a need for detection methods that are label-free and real-time. In this paper, we have selected staphylococcal protein A (SPA) and swine immunoglobulin G (IgG), and monitor the bindings between SPA and swine IgG with different concentrations, as well as the dissociations of SPA-swine IgG complex in different pH values of phosphate buffer by oblique-incidence reflectivity difference (OIRD) in a label-free and real-time fashion. We obtain the ON and OFF reaction dynamic curves corresponding to the bindings and dissociations of SPA and swine IgG. Through our analysis of the experimental results, we have been able to obtain the damping coefficients and the dissociation time of SPA and swine IgG for different pH values of the phosphate buffer. The results prove that the OIRD technique is a competing method for monitoring the dynamic processes of biomolecule interaction and achieving the quantitative information of reaction kinetics.
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Published: 20 January 2015
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| PACS: |
07.60.Fs
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(Polarimeters and ellipsometers)
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81.70.Fy
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(Nondestructive testing: optical methods)
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87.80.Dj
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(Spectroscopies)
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83.85.Ei
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(Optical methods; rheo-optics)
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