One-Step Label-Free Molecular Interaction Kinetic Measurement

Molecular interactions are integral to virtually all biological processes including cell signaling, enzyme activity, protein functionality, and disease development. Understanding the kinetics of these interactions is crucial for providing detailed quantitative and mechanistic insights, at the molecular level, which are essential for advancements in life sciences and biomedical research. Traditional methods for understanding molecular interaction kinetics often produce averaged results from large populations of molecules, thereby obscuring the unique behaviors and complexities of individual molecular interactions and often need separate steps to measure association and dissociation kinetics. Further, they typically rely on labels such as fluorescent probes, nanoparticles or other tabs, which can potentially alter the properties of the molecules under investigation.

 

Researchers at The Biodesign Institute of Arizona State University have developed a new one-step molecular interaction kinetic measurement method, based on label-free real-time optical imaging of the binding and leaving events of individual analyte molecules on a sensor surface. By leveraging kinetics-based information, this method distinguishes specific from nonspecific bindings and accurately determines association and dissociation rates in a single step. This technique is particularly effective for studying weak or complex interactions, as it records and analyzes each interaction at the single-molecule level, offering a significant improvement over conventional approaches.

 

This novel label-free, single-molecule technology is able to effectively image and analyze single molecules and binding kinetics.

 

Potential Applications

Benefits and Advantages

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