Ultrasensitive immunosensing of tuberculosis CFP-10 based on SPR spectroscopy
| Autor: | Cm Kim Cheol-Min Kim, Jaebeom Lee Lee, Jaewook Lee Lee, Hc Shin Hyun-Chul Shin, Hk Park Hye-Kyung Park, Sj Lee Seok Jae Lee, Ys Kim Young Sik Kim, Kwangnak Koh, Sc Hong Seong Cheol Hong, Hx Chen Hongxia Chen, Hj Kim Hwa-Jung Kim, Cl Chang Chulhun L. Chang, T.J. Park |
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| Rok vydání: | 2011 |
| Předmět: |
Materials science
CFP-10 medicine.diagnostic_test Metals and Alloys Nanotechnology Self-assembled monolayer bacterial infections and mycoses Condensed Matter Physics complex mixtures Surfaces Coatings and Films Electronic Optical and Magnetic Materials chemistry.chemical_compound chemistry Cystamine Immunoassay Materials Chemistry medicine Gold surface Electrical and Electronic Engineering Surface plasmon resonance Spectroscopy Instrumentation Biosensor |
| Zdroj: | Sensors and Actuators B: Chemical. 156:271-275 |
| ISSN: | 0925-4005 |
| DOI: | 10.1016/j.snb.2011.04.032 |
| Popis: | An antigen (Ag), CFP-10, found in tissue fluids of tuberculosis (TB) patients may be an ultimate candidate for use as a sensitive TB marker with a sensing method for early simplified diagnosis of TB. In this study, chemical and optical optimizations were carried out using novel immuno-materials for establishment of a self-assembled surface plasmon resonance (SPR) optical immunosensor system for detection of CFP-10, which is valuable for pre-clinical work, prior to conduct of massive clinical observations. For creation of a simple sensing interface, a monoclonal antibody (anti-CFP-10) was immobilized directly on a gold surface, followed by blocking with cystamine. Orientation and accessibility of anti-CFP-10 were assessed by the selective binding of CFP-10. Recent results indicate that the reusability of the sensor chip adopting the cystamine method was found to be preferable to other immobilization methods. A linear relationship was well correlated between SPR angle shift and CFP concentrations in the range from 100 ng mL −1 to 1 μg mL −1 . Modification of the SPR chip with antibody provides a simple experimental platform for investigation of isolated proteins under experimental conditions resembling those of their native environment. |
| Databáze: | OpenAIRE |
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