Getting site-specific with actomyosin inhibitors

Laura K. Gunther, Christopher M. Yengo

Research output: Contribution to journalArticlepeer-review


Actin and myosin play important roles in many devastating diseases and thus are attractive targets for small-molecule therapy. In this issue of JBC, Guhathakurta et al. have developed a high-throughput screening assay to find small molecules that interfere with the actomyosin interaction. They utilized time-resolved FRET (TR-FRET) and a unique donor–acceptor pair (filamentous actin and a peptide that binds near the myosin-binding site on actin) to find novel molecules that interfere with the actomyosin ATPase and alter the structure of actin filaments. These findings demonstrate the power and potential of high-throughput TR-FRET in monitoring molecular interactions.

Original languageEnglish (US)
Pages (from-to)12299-12300
Number of pages2
JournalJournal of Biological Chemistry
Issue number31
StatePublished - Aug 3 2018

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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