Our new paper describing an SPR kinetic assay to monitor PROTAC ternary complexes is now out in ACS Chemical Biology

  • ToC graphics
  • Figure 1. Schematic and binding data illustrating our SPR approach for measuring binding kinetics and determining cooperativity (α) for PROTAC binary and ternary complex formation.
  • Chart 1. PROTACs Utilized in This Study
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Measuring kinetics by surface plasmon resonance (SPR), we reveal how striking differences in stability and lifetime of target:PROTAC:ligase ternary complexes influence initial rates of PROTAC induced protein degradation. Congratulations to Michael, Scott, Claire, Will and our colleagues at Boehringer Ingelheim. Read more about our paper here.

  • Pre-print of this paper was first posted at bioRxiv 451948 on 25 October 2018 doi: https://doi.org/10.1101/451948
  • Selected to be featured in ACS Editors' Choice based on recommendation by ACS journals' editors. Under ACS Editors' Choice, our article has been sponsored for immediate, free open access by ACS due to its potential for broad public interest, an honor given to only one article from the entire ACS portfolio each day of the year.