Competitive inhibition of TRPV1–calmodulin interaction by vanilloids

Anasztázia Hetényi, Lukács Németh, Edit Wéber, Gerda Szakonyi, Zoltán Winter, Katalin Jósvay, Éva Bartus, Zoltán Oláh, Tamás A. Martinek

Research output: Contribution to journalLetter

5 Citations (Scopus)


There is enormous interest toward vanilloid agonists of the pain receptor TRPV1 in analgesic therapy, but the mechanisms of their sensory neuron-blocking effects at high or repeated doses are still a matter of debate. Our results have demonstrated that capsaicin and resiniferatoxin form nanomolar complexes with calmodulin, and competitively inhibit TRPV1–calmodulin interaction. These interactions involve the protein recognition interface of calmodulin, which is responsible for all of the cell-regulatory calmodulin–protein interactions. These results draw attention to a previously unknown vanilloid target, which may contribute to the explanation of the paradoxical pain-modulating behavior of these important pharmacons.

Original languageEnglish
Pages (from-to)2768-2775
Number of pages8
JournalFEBS letters
Publication statusPublished - Aug 1 2016


  • TRPV1
  • calmodulin
  • capsaicin
  • resiniferatoxin
  • vanilloid

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Competitive inhibition of TRPV1–calmodulin interaction by vanilloids'. Together they form a unique fingerprint.

  • Cite this