Binding of tryptamine analogs at h5-HT1E receptors: a structure-affinity investigation

Bioorg Med Chem. 2004 May 15;12(10):2545-52. doi: 10.1016/j.bmc.2004.03.026.

Abstract

Structure-affinity requirements for the binding of serotonin (5-HT) analogs at human 5-HT1E receptors were investigated by examining the affinities of >40 tryptamine-related compounds. No tryptamine analog was found to bind with substantially higher affinity than 5-HT. The results indicate that hydrogen bonding plays a key role in the 5-HT1E/receptor interaction. This finding was supported using quantitative structure-activity analysis (QSAR) techniques such as comparative molecular field analysis (CoMFA) and the program QsarIS.

MeSH terms

  • Cell Line
  • Humans
  • Molecular Conformation
  • Molecular Structure
  • Quantitative Structure-Activity Relationship
  • Radioligand Assay
  • Receptors, Serotonin / metabolism*
  • Serotonin / analogs & derivatives*
  • Serotonin / chemistry
  • Serotonin / metabolism
  • Tryptamines / chemistry*

Substances

  • Receptors, Serotonin
  • Tryptamines
  • serotonin 1E receptor
  • Serotonin
  • tryptamine