Monitoring of interactions between aptamers and human IgE by Surface Plasmon Resonance imaging

Aptamers are in vitro-generated, short, single-stranded nucleic acids that selectively bind to target compounds such as small molecules or proteins1, 2. Their main advantage over monoclonal antibodies is their resistance to denaturation and degradation. Being very robust and easy to synthesize, they are becoming widely used for the development of aptamer-based biosensors in the diagnostics field3.
This application note shows that the HORIBA Scientific SPRi platform is suitable for the analysis of aptamer-based molecular interactions. For this purpose, the interaction between human IgE protein, an antibody involved in allergic reactions, and a human IgE specific aptamer4 is presented as proof-of-concept.