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A biased allosteric modulator is a molecular glue for β 2 AR dimerization

Research Drug Discovery

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TL;DR - A Nature study reports that AP-7-168, an optimized β-arrestin-biased negative allosteric modulator, acts as a molecular glue that stabilizes β2-adrenergic receptor (β2AR) homodimers. This links biased allosteric modulation with direct control of receptor assembly.

  • AP-7-168 is derived from a β-arrestin-biased negative allosteric modulator of β2AR.
  • The compound promotes and stabilizes β2AR homodimerization.
  • The finding identifies a molecular-glue mechanism for modulating a G-protein-coupled receptor.
  • The provided summary does not specify downstream functional effects or therapeutic outcomes.

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A biased allosteric modulator is a molecular glue for β 2 AR dimerization

Nature Jiemin Shen, Teja Nikhil Peddada, Konstantin E. Komolov, Francesco De Pascali, Alexander M. Garces, Haoqing Wang, Muhammad Ehsan, Pil Seok Chae, Michael T. Lerch, Jeffrey L. Benovic, Jun Xu, Brian K. Kobilka 2026-08-19 doi:10.1038/s41586-026-10892-y
Public signals OpenAlex citations 2 · Semantic Scholar citations 2 · Semantic Scholar influential citations 0
Providers: Hugging Face · N/A OpenAlex · Citations 2 Publisher · N/A Semantic Scholar · Citations 2 · Influential citations 0 X · N/A Fetched 2026-09-19 14:26:05.767299 UTC

TL;DR - A Nature study reports that AP-7-168, an optimized β-arrestin-biased negative allosteric modulator, acts as a molecular glue that stabilizes β2-adrenergic receptor (β2AR) homodimers. This links biased allosteric modulation with direct control of receptor assembly.

  • AP-7-168 is derived from a β-arrestin-biased negative allosteric modulator of β2AR.
  • The compound promotes and stabilizes β2AR homodimerization.
  • The finding identifies a molecular-glue mechanism for modulating a G-protein-coupled receptor.
  • The provided summary does not specify downstream functional effects or therapeutic outcomes.
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