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Updated: Apr 22, 2026

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes
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Proximity Binding Assay for PROTAC Ternary Complex Analysis.

Irene Ponzo1, Alice Soldà1, Charlotte Crowe2

  • 1Dynamic Biosensors GmbH Germany, Perchtinger Str. 8-10, 81379 Munich, Germany.

ACS Sensors
|April 21, 2026
PubMed
Summary
This summary is machine-generated.

We developed a novel assay to simultaneously measure binary and ternary interactions for targeted protein degradation drug discovery. This method aids in developing improved Proteolysis Targeting Chimeras (PROTACs) and molecular glues.

Keywords:
BETBRDCRBNPROTACVHLY-structureaffinityaviditykineticsmolecular glueswitchSENSEtargeted protein degradationternary complex

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Targeted protein degradation using Proteolysis Targeting Chimeras (PROTACs) and molecular glues relies on ternary complex formation.
  • Analyzing these ternary interactions is crucial but challenging in drug discovery.

Purpose of the Study:

  • To introduce a novel proximity binding assay for simultaneous measurement of binary and ternary interaction kinetics.
  • To facilitate the development of PROTACs and molecular glues by providing insights into proximity-mediated binding.

Main Methods:

  • A Y-shaped DNA scaffold tethers target proteins and ubiquitin E3 ligase subunits.
  • PROTAC-induced ternary complex formation is measured using Förster Resonance Energy Transfer (FRET).
  • Binary interactions are detected via fluorescence quenching; the assay supports high-throughput analysis.

Main Results:

  • The assay successfully measured kinetics for cereblon (CRBN) and von Hippel-Lindau (VHL) E3 ligase receptors with various PROTACs and bromodomain targets.
  • Automated workflows enabled real-time analysis of 384 sensorgrams in a single run with picomole quantities.
  • Demonstrated the assay's capability for simultaneous binary and ternary interaction kinetic measurements.

Conclusions:

  • The developed proximity binding assay is effective for characterizing PROTAC and molecular glue interactions.
  • This assay provides valuable insights into proximity-mediated binding kinetics for optimizing targeted protein degradation strategies.
  • Enables accelerated development of next-generation PROTACs and molecular glues.