Assembly and Characterization of a Slingshot DNA Nanostructure for the Analysis of Bivalent and Bispecific Analytes with Biosensors.

The characterization of novel therapeutic antibodies with multivalent or multispecific binding sites requires new measurement modalities for biosensors, to discriminate the engagement of antigens via one, two, or even more binding moieties. The presentation of antigens on a sensor surface in a well-controlled spatial arrangement is a prerequisite for the successful interpretation of binding kinetics measurements of multivalent analytes, but the adjustment of defined distances between immobilized ligands is difficult to achieve in state-of-the-art biosensor systems. Here, we introduce a simple DNA nanostructure resembling a slingshot, which can be configured with two identical or two different antigens (bivalent or bispecific), which are spaced at a defined distance.

Suppression of Photoanodic Surface Oxidation of n-Type 6H-SiC Electrodes in Aqueous Electrolytes.

The photoelectrochemical characterization of silicon carbide (SiC) electrodes is important for enabling a wide range of potential applications for this semiconductor. However, photocorrosion of the SiC surface remains a key challenge, because this process considerably hinders the deployment of this material into functional devices. In this report, we use cyclic voltammetry to investigate the stability of n-type 6H-SiC photoelectrodes in buffered aqueous electrolytes.

Protein analysis by time-resolved measurements with an electro-switchable DNA chip.

Measurements in stationary or mobile phases are fundamental principles in protein analysis. Although the immobilization of molecules on solid supports allows for the parallel analysis of interactions, properties like size or shape are usually inferred from the molecular mobility under the influence of external forces. However, as these principles are mutually exclusive, a comprehensive characterization of proteins usually involves a multi-step workflow.

Quantitation of affinity, avidity, and binding kinetics of protein analytes with a dynamically switchable biosurface.

A label-free method for the analysis of interactions of proteins with surface-tethered ligands is introduced. Short DNA levers are electrically actuated on microelectrodes by ac potentials, and their switching dynamics are measured in real-time by fluorescence energy transfer. Binding of proteins to ligands attached to the top of the DNA levers is detected by time-resolved measurements of the levers' dynamic motion.