Please join Carterra at our upcoming symposium in Boston, MA.
You will spend the day learning about high-throughput drug discovery with some of the industry’s leading scientists. Our speakers will present new ways of looking at discovery, applications, and workflows, including HT-SPR. The topics you'll hear about include:
Network with your peers. Lunch will be provided. Registration is required as seating is limited.
Companies presenting in 2025:
Agenda |
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9:45 – 10:00 AM |
Arrive and Check-in |
10:00 – 10:30 AM |
Networking and Coffee/Tea |
10:30 – 10:45 AM |
Symposium Begins—Welcome |
10:45 – 11:15 AM |
![]() High-throughput Recombinant Antibody Validation for Community Distribution |
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Abstract: The Institute for Protein Innovation (IPI) is a non-profit research organization providing recombinant antibodies to the biomedical community against understudied targets. Antibodies are produced using a yeast display platform, and rigorous QC and validation are performed to ensure highest quality. High-throughput surface plasmon resonance (SPR) is performed to assess binding affinity and kinetics, alongside polyreactivity, flow cytometry, immunofluorescence (IF) and other application assay testing. Cross-reactivity analysis ensures specificity among related proteins. Validated antibodies are distributed via Addgene, enabling broad scientific impact. This presentation highlights high-throughput SPR and antibody characterization using the Glypican protein family as an example. |
11:15 – 11:45 AM |
![]() High-Throughput VHH Nanobody Discovery: Integrating Machine Learning with Rapid Cell-Free Expression |
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Abstract: We combine machine learning and cell-free expression to rapidly develop and optimize VHH nanobodies, enabling the assessment of nearly 200 potential binders per day—from DNA to binding kinetics. Our ML-driven models propose novel CDR sequences predicted to enhance affinity and specificity, which are quickly synthesized and screened via surface plasmon resonance. This streamlined workflow initially identifies monomeric VHHs and then extends to bi-specific constructs by combining multiple binders. The resulting data is continually fed back into our machine learning pipeline, refining subsequent rounds of nanobody design. We will present data illustrating the speed, flexibility, and potential impact of this integrated approach on nanobody discovery for both therapeutic and diagnostic applications. |
11:45 AM - 12:15 PM |
![]() Customized Workflows Accelerate Immunoassay Development with High-Content Biophysics and Modeling |
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Abstract: Immunoassays enable precise characterization of biological systems and deepen the understanding of disease, empower diagnosis, and quantify therapeutic effects. The continuous need for enhanced performance imposes demands on the development pipelines and the molecular tools that power immunoassay technologies. Here, bottlenecks arise from classically low-throughput development processes and unclear relationships between molecular attributes and performance specifications. In this seminar, I present customized workflows that accelerate immunoassay development with our extensive collections of biomarker-specific antibodies, information-rich datasets, and predictive modeling. I show how these intelligently-guided, rule-based workflows efficiently traverse the complex combinatorics of immunoassay formulation and development, delivering multifactor, next-generation performance. |
12:15 – 1:30 PM |
Lunch and Networking |
1:30 – 2:00 PM |
![]() Effect of the membrane proximal region on the antigenic structure of herpes simplex virus glycoproteins gD, gC, and gE |
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Abstract: Herpes simplex virus (HSV) types 1 and 2 contain multiple glycoproteins on its membrane surface to facilitate virus entry, cell-cell spread, and immune evasion. gD is the receptor-binding protein and initiates the virus-cell fusion process. gE is involved in cell-cell spread and works in immune evasion by binding an antibody’s Fc domain. gC is important for virus attachment and inhibits complement activation by binding C3b. Modifications of these three glycoproteins form the basis of an HSV-2 vaccine currently in human trials (BNT163, NCT0543258). We asked whether the inclusion of the membrane proximal region (MPR) of each protein would affect their antigenic properties. We created detailed antigenic maps for soluble forms of gD, gC, and gE, both with and without the MPRs. Kinetic analysis of the glycoproteins using HT-SPR suggested differences in MAb-gD avidity depending on gD length. In addition, multiple MAbs displayed significant kinetic differences between the gE forms. Our data suggest that the addition of the 14 membrane proximal region residues to gE and 10 residues to gD affect their antigenic structure. |
2:00 – 2:30 PM |
![]() Applications from mAbs to Fragment Screening: How Carterra LSA, LSAXT and Ultra HT-SPR Platforms Enable Highly Parallel Analysis Advancing All Drug Discovery Modalities |
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Abstract: Carterra’s HT-SPR technology platforms have set the bar for throughput and scalability for biologics discovery and now extend to small molecule and fragment screening. The Carterra Ultra enables a transformative approach to library screening, highly parallel analysis, where many targets can be screened simultaneously against a library. Why run single campaigns when you can screen your entire target backlog simultaneously? This presentation will highlight three interesting application examples: the detailed kinetic characterization of human Fab fragments directly from bacterial extracts, the profiling of binding of TCRs to arrays of immobilized pMHCs, and fragment library screening. |
2:30 PM |
Symposium Ends |