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Updated: Oct 17, 2025
Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
Published on: April 17, 2017
Rapid conversion of IgG to biosensor using an antibody-binding protein-based probe
Guangwei Zhao1, Haimei Li1, Baowei Li1
1Key Laboratory for Antibodies Medicine, School of Life Science and Technology, Weifang Medical University, Weifang 261053, China. dongjh@wfmc.edu.cn.
We successfully developed a fluorescent probe that can quickly convert full-length antibodies to Quenchbodies, which represent a type of fluorescent immunosensor with high binding affinity and specificity depending on the reaction of antigens and antibodies. An anti-testosterone IgG was successfully converted to an immunosensor that detects testosterone with a limit of detection (LOD) of 0.76 nM and concentration for 50% of maximal effect (EC50) of 61.5 nM. Another IgG-based immunosensor detected ractopamine with an LOD of 15.5 pM and EC50 of 48.6 nM.
We successfully developed a fluorescent probe that can quickly convert full-length antibodies to Quenchbodies, which represent a type of fluorescent immunosensor with high binding affinity and specificity depending on the reaction of antigens and antibodies. An anti-testosterone IgG was successfully converted to an immunosensor that detects testosterone with a limit of detection (LOD) of 0.76 nM and concentration for 50% of maximal effect (EC50) of 61.5 nM. Another IgG-based immunosensor detected ractopamine with an LOD of 15.5 pM and EC50 of 48.6 nM.
