Building Confidence Early in Drug Discovery

Biophysical discovery lives or dies on reagent quality. Get it right from the start, and everything downstream, including kinetics and affinity analysis, can be achieved faster and with greater confidence. Whether you need to de-risk difficult reagents, unlock new modalities, or simply accelerate biophysical discovery – this is the right event for you. During the webinar Sygnature Discovery, Fida Biosystems and Cytiva show how combining FIDA™ (Flow Induced Dispersion Analysis) with Biacore™ SPR in one workflow can speed up and de-risk campaigns at the source and open the door to targets and modalities that were previously hard to reach. Increasingly, drug discovery campaigns are prioritising more challenging targets in important and underserved therapeutic areas. This poses a range of challenges for organisations aiming to rapidly, and successfully, identify and develop novel therapeutics. Having the right tools in place to tackle challenging targets is essential, both to ensure the stability and quality of the reagents going into the screen and for validating identified hits in an efficient and effective manner. This is where FIDA and Biacore SPR systems are particularly powerful. By utilising the strengths of FIDA and SPR, (often in tandem with other technologies such as ASMS), we can enable highly sensitive and efficient biophysical screening workflows, from reagent assessment and QC using FIDA through to the collection of information rich data for qualified hits though SPR, all with the goal of finding the best quality starting points for further development. Here, we take two case studies and look at both a multi-technology hit finding approach and the assessment of a membrane protein target, demonstrating how this strategy has been employed successfully to enable assays, identify novel hits, characterise binding modes, and prioritise molecules for further testing. Why attend? Are you struggling with difficult-to-analyse molecules, challenges in developing robust assays, or unexpected results that don't match theory? Through case studies from Sygnature Discovery, this webinar will demonstrate how combining FIDA and Biocore SPR within a hit discovery workflow can help address these challenges and generate higher-confidence data. Join this session to learn how to uncover the root causes behind challenging sensorgrams, improve assay robustness, and gain deeper insight into molecular interactions to generate more reliable and actionable results. Technologies: · FIDA™ (Flow Induced Dispersion Analysis) technology allows you to measure molecular size and molecular interactions in real time, directly in solution, using the phenomenon of Taylor dispersion. Here, a nanolitre-scale sample is introduced into a controlled laminar flow within a narrow capillary, where the molecules disperse as they travel. The degree of dispersion is governed by how fast the molecules diffuse, which yields their absolute hydrodynamic radius without calibration or reference standards. When a molecule binds a partner it grows larger, so the same measurement returns binding affinity (from picomolar to millimolar Kd) together with kinetics, in minutes and from only nanograms of protein. Working entirely in solution, FIDA reports size, aggregation, oligomerisation, and polydispersity in that single run, directly in complex samples such as cell lysate or serum and on challenging targets and novel modalities including membrane proteins and engineered antibodies. · Biacore™ SPR technology is a label-free, real-time analytical platform used to study biomolecular interactions. It enables researchers to measure how molecules bind to and dissociate from one another, providing detailed information about affinity, binding kinetics, concentration, specificity, and comparability without the need for fluorescent or radioactive labels. Concentrations in the picomolar to nanomolar range in the bulk sample solution can be detected. At the core of the technology is surface plasmon resonance (SPR), an optical phenomenon that detects changes in refractive index at the surface of a sensor chip. In a typical experiment, one interaction partner (the ligand) is immobilized on the sensor chip surface, while the other partner (the analyte) flows across it through a microfluidic system. When binding occurs, the increase in mass at the sensor surface changes the SPR signal, allowing interactions to be monitored continuously in real time.