Quickly rank large pools of antibody candidates
Elucidate binding effects of antibodies within the 2D membrane-constrained cellular environment, taking into account the effects of epitope, steric hindrance, and multivalency.
Part of:
Why Cell Avidity?
Keeping up with the complexity of binding mechanisms
Many immunotherapies adapt to solve the field’s most pressing issues (an intricate balance between persistence, potency, and safety) by integrating multiple signaling mechanisms and engaging with more than one domain (e.g., biparatopic and polyvalent antibodies). With that trend, the binding mechanisms between binder and target also complexify.
Molecular binding assays like tetramer binding and surface plasmon resonance (SPR) measure preconditions for binding, providing limited insights into actual cell binding. Focusing on isolated ligand-receptor interactions or abundance on a molecular level, they can miss the cellular context and often do not correlate well with functional outcomes.
Overcome these challenges with Cell Avidity:
- Generate direct, physiologically relevant measurements of binding in its full, dynamic complexity
- Understand the mechanism of action of your therapeutic products by revealing its complex binding dynamics
- Balance potency and safety by optimizing binding
Cell Avidity measures true binding of biparatopic antibodies
Mechanistic issues limit the effectiveness of many current cancer-targeting antibody therapies, with monospecific antibodies often hindered by receptor dimerization and activation. Biparatopic antibodies, which bind to two unique non-overlapping epitopes, offer a promising solution with stronger binding, more potent antagonism, and higher specificity.
Case study
FGFR2 fusion genes confer sensitivity to FGFR2 kinase inhibitors like Pemigatinib, which saw accelerated FDA approval. However, response rates are hampered by tumor resistance from arising FGRF2 mutations. The researchers showed that the ECD of FGFR2 is necessary for a full oncogenic transformation by FGFR2 fusion. This makes the ECD a promising target for antibody therapies. Biparatopic antibodies present a promising opportunity for targeting FGFR2 owing to increased binding, specificity, and lower likelihood of inter-protein crosslinking. It was hypothesized that the most effective biparatopic antibodies would show both high affinity and high Cell Avidity.
Binding affinity and avidity screening of biparatopic antibodies candidates. Cell Avidity assay shows increased avidity (% bound beads) of biparatopic antibodies (blue/purple) compared to monospecifi c antibodies B, C and D (grey).
Overview of the experimental setup. Left: Visualization of the monospecific antibody epitope sites (A-F) mapped to the FGFR2 extracellular domain (ECD). Center: workflow representation of the generation of the 15 biparatopic antibodies (A/B to E/F) from their monospecific constituent parts (illustrated by F40SL + K409R) by controlled Fab-arm exchange. Right: Viability assay output comparing the 15 biparatopic antibodies with the 6 monospecific antibodies (and an IgG1 negative control) on their growth inhibition of FGFR2-fusion-driven BaF3 cells.
Explore further
Cell Avidity measures true binding of biparatopic antibodies
App Notes
Mechanistic issues limit the effectiveness of many current cancer-targeting antibody therapies, with monospecific antibodies often hindered by receptor dimerization and activation. Biparatopic antibodies, which bind to two unique non-overlapping epitopes, offer a promising solution with stronger binding, more potent antagonism, and higher specificity.
Solutions
Avidion
The next generation Cell Avidity platform
Ideal for cell therapy candidate screening and large characterization studies. Run up to 4 disposable 48-well cartridges a day for a total of 192 measurements with <80 min. hands-on time.
Avidigo
White glove Cell Avidity services
Full-service contract research from experimental design to data report based on Cell Avidity measurements at high throughput.
z-Movi
For small sized Cell Avidity studies
A fast and simple solution for single-sample Cell Avidity experiments. Run up to 20 measurements per day.
Technical note:
These cards are NOT components because they use the finsweet nested collection logic. To pull in the posible multiple people wo worked on it.
This type of 1-many relation is not supported native in Webflow.
Also this section is hidden when emtpy. To keep everything visible here, that is being done outside the webflow designer from within Slater.
These cards are NOT components because they use the finsweet nested collection logic. To pull in the posible multiple people wo worked on it.
This type of 1-many relation is not supported native in Webflow.
Also this section is hidden when emtpy. To keep everything visible here, that is being done outside the webflow designer from within Slater.
Text Link
Identification of potent biparatopic antibodies targeting FGFR2 fusion driven cholangiocarcinoma
Chaturantabut, S. et al.
2025
J. Clin. Investigation
https://www.jci.org/articles/view/182417
Publication
SITC 2025
Conference
April 22, 2025
01-01-20
CAR-TCR Summit 2025
Conference
April 22, 2025
01-01-20
CICON 2025
Conference
April 22, 2025
01-01-20
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