Structure-affinity relationships of indole-based melatonin analogs

Biol Signals Recept. 1999 Jan-Apr;8(1-2):15-23. doi: 10.1159/000014564.

Abstract

This paper reviews our progress made in characterizing structure-affinity relationships of indole-based melatonin analogs. Evidence is presented suggesting a preferred folded conformation for the amido side chain, almost orthogonal to the plane of indole. A 3D-QSAR comparative molecular field analysis (CoMFA) model, accounting for the observed differences in binding affinity within different classes of melatonergic ligands, and capable of quantitatively predicting the binding affinity of new compounds, is also reported.

Publication types

  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Brain / metabolism
  • Drug Design
  • Humans
  • In Vitro Techniques
  • Indoles / chemistry
  • Indoles / metabolism
  • Kinetics
  • Ligands
  • Melatonin / analogs & derivatives*
  • Melatonin / chemistry
  • Melatonin / metabolism
  • Models, Molecular
  • Molecular Conformation
  • Receptors, Cell Surface / metabolism
  • Receptors, Cytoplasmic and Nuclear / metabolism
  • Receptors, Melatonin
  • Structure-Activity Relationship

Substances

  • Indoles
  • Ligands
  • Receptors, Cell Surface
  • Receptors, Cytoplasmic and Nuclear
  • Receptors, Melatonin
  • Melatonin