SLAS 2026

Poster sessions

Poster 1 Title: Massively Parallel SPR-Based Fragment Screening of Kinase Arrays

Presenter: Rebecca L. Rich, PhD Director of Science, Carterra

Poster Number: 1349-E

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

Presenter: Maria McGresham, Ph.D., Senior Applications Scientist, Carterra

Poster Number: 1337-C 

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.

Poster 3 Title: Strategies for Scalable and Sensitive Determination of High Affinity and Slow Dissociating Binding Interaction Kinetics in Antibody Discovery

Presenter: Maria McGresham, Ph.D., Senior Applications Scientist, Carterra

Poster Number: 1409-E

Abstract:Monoclonal antibodies are powerful tools for therapeutic and diagnostic applications and binding kinetics is an important element of the potency and efficacy of these molecules. Many antibodies and optimized therapeutics show very high affinities with stable dissociation kinetics, and these high affinity interactions represent a challenge for accurate measurement using real time SPR binding studies, as slow dissociation yields minimal signal change over typical time courses. This poster explores two effective strategies using HT-SPR to measure slow dissociation of many interactions in parallel and with high sensitivity. The most sensitive and simple approach is the use of a chase injection to measure surface occupancy after a long dissociation period. The other is the use of both short and long dissociation times, which can enable an extended dissociation phase without excessively extending the overall length of an experiment. Both these approaches can be implemented at scale for the screening and characterization of hundreds to thousands of high affinity interactions using Carterra HT-SPR platforms.