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Unraveling the Dynamics of Antibody-Antigen Interaction by DNA Origami
1State Key Laboratory of Chemo/Bio-sensing and Chemometrics, College of Chemistry and Chemical Engineering, Hunan Provincial Key Laboratory of Biomacromolecular Chemical Biology, Hunan University, Changsha, 410082 P. R. China.
To investigate the dynamic interaction between antibody and antigen, Fan et al. rationally designed a triangular DNA origami framework to spatially organize the antigenic epitopes at the nanoscale and thus to monitor the transient binding kinetics of the dynamic antigen-antibody complexes at room temperature. This study provides a straightforward, designable and programmable strategy to investigate the transition kinetics of antibody-antigen interaction at a single-molecule level and improve the understanding toward the design of the next-generation antibodies and vaccines for various biomedical applications. This work has been published online in Nature Communications on June 19, 2020.
To investigate the dynamic interaction between antibody and antigen, Fan et al. rationally designed a triangular DNA origami framework to spatially organize the antigenic epitopes at the nanoscale and thus to monitor the transient binding kinetics of the dynamic antigen-antibody complexes at room temperature. This study provides a straightforward, designable and programmable strategy to investigate the transition kinetics of antibody-antigen interaction at a single-molecule level and improve the understanding toward the design of the next-generation antibodies and vaccines for various biomedical applications. This work has been published online in Nature Communications on June 19, 2020.
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Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

