Structural determinants for histamine H(1) affinity, hERG affinity and QTc prolongation in a series of terfenadine analogs

Bioorg Med Chem Lett. 2009 Sep 1;19(17):5043-7. doi: 10.1016/j.bmcl.2009.07.047. Epub 2009 Aug 5.

Abstract

In the late 1980's reports linking the non-sedating antihistamines terfenadine and astemizole with torsades de pointes, a form of ventricular tachyarrhythmia that can degenerate into ventricular fibrillation and sudden death, appeared in the clinical literature. A substantial body of evidence demonstrates that the arrhythmogenic effect of these cardiotoxic antihistamines, as well as a number of structurally related compounds, results from prolongation of the QT interval due to suppression of specific delayed rectifier ventricular K+ currents via blockade of the hERG-IKr channel. In order to better understand the structural requirements for hERG and H(1) binding for terfenadine, a series of analogs of terfenadine has been prepared and studied in both in vitro and in vivo hERG and H(1) assays.

MeSH terms

  • Animals
  • Electrocardiography
  • Guinea Pigs
  • Histamine H1 Antagonists, Non-Sedating / chemical synthesis
  • Histamine H1 Antagonists, Non-Sedating / chemistry*
  • Histamine H1 Antagonists, Non-Sedating / pharmacology
  • Humans
  • Protein Binding
  • Receptors, Histamine H1 / metabolism*
  • Structure-Activity Relationship
  • Terfenadine / analogs & derivatives*
  • Terfenadine / chemistry
  • Terfenadine / pharmacology
  • Trans-Activators / metabolism*
  • Transcriptional Regulator ERG

Substances

  • ERG protein, human
  • Histamine H1 Antagonists, Non-Sedating
  • Receptors, Histamine H1
  • Trans-Activators
  • Transcriptional Regulator ERG
  • Terfenadine