LSPR biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex
Herein we demonstrate a sensitive approach for protein detection based on peak shifts of localized surface plasmon resonance (LSPR) induced by aptamer–antigen–antibody sandwich structures. The applicability of the proposed method is demonstrated using human α-thrombin as a model analyte. While the b...
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sg-ntu-dr.10356-1004852020-03-07T11:35:30Z LSPR biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex Guo, Longhua Kim, Dong-Hwan School of Chemical and Biomedical Engineering Herein we demonstrate a sensitive approach for protein detection based on peak shifts of localized surface plasmon resonance (LSPR) induced by aptamer–antigen–antibody sandwich structures. The applicability of the proposed method is demonstrated using human α-thrombin as a model analyte. While the binding of thrombin to its specific receptor, thrombin binding aptamer (TBA) modified on Au nanorods (AuNRs), causes a measurable LSPR shift, a subsequent binding of an anti-thrombin antibody to the captured thrombin can exhibit a nearly 150% amplification in the LSPR response. This enhanced signal essentially leads to an improvement of limit of detection (LOD) by more than one order of magnitude. In addition, the use of TBA as thrombin recognition units makes the biosensor reusable. The feasibility of the proposed method was further exploited by the detection of thrombin in human serum, opening the possibility of a real application for diagnostics and medical investigations. 2013-07-10T02:10:06Z 2019-12-06T20:23:18Z 2013-07-10T02:10:06Z 2019-12-06T20:23:18Z 2011 2011 Journal Article Guo, L., Kim, D.-H. (2011). LSPR biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex. Biosensors and Bioelectronics, 31(1), 567-570. https://hdl.handle.net/10356/100485 http://hdl.handle.net/10220/11078 10.1016/j.bios.2011.10.047 en Biosensors and bioelectronics © 2011 Elsevier B.V. |
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Herein we demonstrate a sensitive approach for protein detection based on peak shifts of localized surface plasmon resonance (LSPR) induced by aptamer–antigen–antibody sandwich structures. The applicability of the proposed method is demonstrated using human α-thrombin as a model analyte. While the binding of thrombin to its specific receptor, thrombin binding aptamer (TBA) modified on Au nanorods (AuNRs), causes a measurable LSPR shift, a subsequent binding of an anti-thrombin antibody to the captured thrombin can exhibit a nearly 150% amplification in the LSPR response. This enhanced signal essentially leads to an improvement of limit of detection (LOD) by more than one order of magnitude. In addition, the use of TBA as thrombin recognition units makes the biosensor reusable. The feasibility of the proposed method was further exploited by the detection of thrombin in human serum, opening the possibility of a real application for diagnostics and medical investigations. |
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School of Chemical and Biomedical Engineering |
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School of Chemical and Biomedical Engineering Guo, Longhua Kim, Dong-Hwan |
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Guo, Longhua Kim, Dong-Hwan |
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Guo, Longhua Kim, Dong-Hwan LSPR biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex |
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Guo, Longhua |
title |
LSPR biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex |
title_short |
LSPR biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex |
title_full |
LSPR biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex |
title_fullStr |
LSPR biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex |
title_full_unstemmed |
LSPR biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex |
title_sort |
lspr biomolecular assay with high sensitivity induced by aptamer–antigen–antibody sandwich complex |
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2013 |
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https://hdl.handle.net/10356/100485 http://hdl.handle.net/10220/11078 |
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