싸토리우스코리아

Overview

To choose the best lead candidates during drug and antibody screening, scientists characterize a molecule’s binding properties, such as kinetics and affinity. Robust assay design reduces experimental artifacts caused by avidity and enables researchers to determine binding kinetics and affinity values. Understanding the differences between affinity and avidity is essential when designing and developing kinetic binding assays.

In this webinar, Tim Heiseler - Senior Application Scientist at Sartorius - discusses the phenomena of affinity and avidity as measured in label-free biomolecular interaction analysis and explain how to recognize and resolve problems arising from interactions that contain bivalent or multivalent molecules.

Document type: Webinar
View time: 26 minutes

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Key Takeaways

Topics discussed:

Clarifying and demonstrating binding affinity and avidity
Identifying multivalent analyte interactions and assay design considerations
Optimizing assays to avoid artifacts in biomolecular interaction analysis
Introducing ChromoTek’s nanobodies and the Spot-Tag^® system

Affinity versus Avidity: Differentiating Between Binding Phenomena Webinar

Overview

Key Takeaways

Webinar Speakers

Tim Heiseler, PhD

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