Drug Discovery Chemistry 2026

Poster sessions

Poster 1 Title: HT-SPR Screening and Kinetic Characterization of Small-Molecule Binders Using Carterra Vega™ and Comparison with AI Binding Predictions

Poster number: P012

Abstract: Carterra Vega™ is a high-throughput surface plasmon resonance (HT-SPR) platform that enables 48-analyte parallel analysis through its multi-channel flow cell, supporting high-quality binding data collection for up to two targets plus an internal reference in each channel. In this study, small-molecule compounds from the Maybridge fragment library were screened against human carbonic anhydrase II (hCAII) and XII (hCAXII) using Vega, allowing a 384-well plate to be screened in approximately 35 minutes while providing kinetic context. With fast cycle times and an optional integrated plate-loading robot, Vega can screen more than 20,000 compounds per day. SPR screening results were compared with binding predictions generated using Boltz-2, and selected hits were subsequently characterized by titration experiments to determine kinetic and affinity parameters. The comparison showed agreement between predicted and experimentally observed binders for a subset of compounds, while also revealing additional binders that were not strongly predicted by the model. Further analysis suggests that AI-based binding predictions align well with known chemical patterns represented in available data, while SPR screening can reveal additional binders beyond those learned patterns. Together, these results demonstrate how HT-SPR can efficiently identify and characterize small-molecule binders while generating experimental datasets that complement and inform computational prediction approaches in early drug discovery.

Poster 2 Title: Massively Parallel SPR-Based Fragment Screening of Kinase Arrays

Poster Number: P013

Abstract: Kinases provide a wealth of opportunities for addressing human disease, but their presence in so many critical cellular functions presents challenges for developing drugs with the proper selectivity profiles for maximal therapeutic, and minimal toxic, effect. Direct label-free approaches, such as SPR, can complement activity assays by providing the intrinsic affinity, while observing the real-time kinetics, of interactions. In this poster, we highlight the power of combining an extensive panel of ready-made biotinylated kinases with HT-SPR to generate a wealth of compound binding information that can augment the drug discovery process with broader selectivity profiling in less time for less cost. Here we highlight the power of combining an extensive panel of ready-made biotinylated kinases with HT-SPR to generate a wealth of compound binding information. In three days over 125,000 interactions were measured between a panel of kinases and the Maybridge 1000 fragment library. We also profiled a kinase-focused small molecule library and obtained more than 80,000 binding interactions in a three-day instrument run. Detailed kinetics were then subsequently obtained for hits of interest. Beyond simple yes/no reporting, this approach allows for nuanced kinetic profiling for up to hundreds of binding events in parallel, thereby enabling thoughtful discovery of safe and efficacious drug candidates.

Poster 3 Title: Increasing DNA Encoded Library Screening Resolution Using HT-SPR

Poster Number: P014

Abstract: DNA encoded library (DEL) technology has permitted substantial leaps in compound screening by enabling a more facile way to interrogate libraries and develop lead compounds. While a huge benefit to DEL technology is its reduction in the sheer number and tracking of discrete compounds through the screening process, it does come with a limitation in binding properties that can be gleaned for potential hits. In practice, from an initial screen numbering millions, the resulting thousands of hits are then reduced to around 50 compounds carried forward into downstream assays without any detailed characterization of their binding properties. These fundamental binding properties include kinetics as well as the target binding site. To address this resolution gap in DEL screening, demonstrated here is a technique to further characterize hits with improved resolution using high-throughput surface plasmon resonance (HT-SPR). HT-SPR characterizes the full kinetic profile for both weak and strong binders. Assay resolution can be further increased by inclusion of high-homology family members, truncated or mutated forms, binding partner disruption, etc., yielding a richer profile of lead candidates. With a screening capacity of thousands per week, HT-SPR affords a high-resolution technique that matches the throughput needs in this phase of discovery between the full library and a handful of leads. Additionally, this approach can work with any moiety having DNA attachment, including screening for targeted protein degraders (TPDs) and macrocycles.