Tuesday, August 5, 8 AM PST | 11 AM EST

Understanding cytokine–receptor interactions is critical for advancing immunology research and therapeutic development, but capturing these interactions in a native-like state on the cell surface can be challenging.

In this webinar, Conigen Bioscience’s Assay Development Scientist, Dr. Alyssa Ball, will share how the team leveraged Nicoya’s Alto™ digital surface plasmon resonance (SPR) system to characterize cytokine–receptor binding kinetics using novel soluble homo- and heterodimeric cytokine receptors that mimic their natural conformation on the cell surface. The cytokine–receptor binding analysis will be demonstrated using two examples: the Type II interferon γ (IFNγ) receptor 1 (IFNγR1) homodimer and the Type I interferon α/β receptor (IFNαR) heterodimer.

By mimicking the natural dimeric conformations of cytokine receptors, these proteins achieve significantly enhanced binding potency to their respective cytokines (i.e., IFNγ and Type I IFN)—insights made possible by Alto’s real-time, label-free analysis in a high-throughput, digital format.

Prior to Dr. Alyssa Ball’s presentation, Nicoya’s Head of Application Development, Dr. Michael Piazza, will give an overview of Nicoya’s Alto™ digital SPR system and the recently acquired Applied Photophysics product portfolio.

Topics covered in this webinar:

• How Conigen Bioscience’s innovative soluble protein dimers enhance ligand-binding sensitivity and potency of cytokine–receptor interactions

• Why SPR was critical for revealing nuanced differences in binding potency

• How Alto digital SPR enables rapid, high-quality kinetic data for complex receptor–ligand systems

• How real-time, label-free kinetic analysis combined with structural and stability characterization can accelerate the selection of functionally relevant and stable therapeutic candidates

Whether you’re working in basic immunology, structural biology, or drug discovery, this webinar will highlight how Conigen’s novel soluble dimeric proteins – engineered to mimic native receptor conformations – can significantly enhance binding potency and enable more accurate characterization of complex protein interactions.