Targeted protein degradation proved a small molecule could eliminate a disease-causing protein instead of blocking it. RIPTACs™, or Regulated Induced Proximity Targeting Chimeras, sit within that same induced proximity category but work differently: a heterobifunctional molecule holds a tumor-specific target protein and a separate, pan-essential effector protein together in a cooperative ternary complex, silencing the essential protein only in cells carrying the target. Nothing gets degraded. It's a hold-and-kill mechanism, and it's already in patients. An AR-BRD4 RIPTAC™ built on this approach is in a Phase 1/2 trial for metastatic castration-resistant prostate cancer, with meaningful PSA declines reported even in patients whose disease had already progressed on prior treatment.
Join Promega and ICE Bioscience in this co-hosted webinar on characterizing a RIPTAC™ mechanism like this one, using AR-BRD4 system as an example.
In this webinar, you will:
Learn how NanoBRET® characterizes the "hold" mechanism by measuring RIPTAC™ ternary complex formation and target engagement in live cells
Explore how an AR-BRD4 case study defines the "kill" response through AR-dependent growth inhibition, together with downstream biomarker modulation.
See how a staged in vitro to in vivo assay strategy moves RIPTAC™ candidates beyond mechanistic validation toward developability and translational assessment
Discover how flexible assay development capabilities can accelerate the evaluation of emerging RIPTAC™ and induced-proximity programs
