An electrochemical sensor based on the human estrogen receptor ligand binding domain

Nano Lett. 2007 Sep;7(9):2831-4. doi: 10.1021/nl071451l. Epub 2007 Jul 26.

Abstract

Three different conformations of the ligand binding domain of the human estrogen receptor (ER-LBD) are observed for the native state when binding an agonist and when binding an antagonist. By conjugating ER-LBD conformation specific peptides to CdS nanoparticles, the three different states can be identified by anodic stripping voltammetry. This electrochemical sensor can detect and distinguish the binding of different ligands to the human estrogen receptor.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Biosensing Techniques / instrumentation*
  • Biosensing Techniques / methods
  • Cadmium Compounds / chemistry
  • Equipment Design
  • Equipment Failure Analysis
  • Estrogen Receptor Modulators / analysis*
  • Estrogen Receptor Modulators / chemistry*
  • Humans
  • Nanostructures / chemistry*
  • Nanotechnology / instrumentation*
  • Nanotechnology / methods
  • Protein Binding
  • Protein Interaction Mapping / instrumentation*
  • Protein Interaction Mapping / methods
  • Quantum Dots
  • Receptors, Estrogen / analysis
  • Receptors, Estrogen / antagonists & inhibitors*
  • Sulfides / chemistry

Substances

  • Cadmium Compounds
  • Estrogen Receptor Modulators
  • Receptors, Estrogen
  • Sulfides
  • cadmium sulfide