An electrochemical sensor based on the human estrogen receptor ligand binding domain.
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.
Hansen
Jacob A
JA
Department of Chemistry, Aarhus University, 8000 Aarhus C, Denmark.
Sumbayev
Vadim V
VV
Gothelf
Kurt V
KV
D001665:Binding Sites; D015374:Biosensing Techniques / Q000295:instrumentation* / Q000379:methods; D019187:Cadmium Compounds / Q000737:chemistry; D004867:Equipment Design; D019544:Equipment Failure Analysis; D020847:Estrogen Receptor Modulators / Q000032:analysis* / Q000737:chemistry*; D006801:Humans; D049329:Nanostructures / Q000737:chemistry*; D036103:Nanotechnology / Q000295:instrumentation* / Q000379:methods; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000295:instrumentation* / Q000379:methods; D045663:Quantum Dots; D011960:Receptors, Estrogen / Q000032:analysis / Q000037:antagonists & inhibitors*; D013440:Sulfides / Q000737:chemistry
D019187:Cadmium Compounds; D020847:Estrogen Receptor Modulators; D011960:Receptors, Estrogen; D013440:Sulfides; C034939:cadmium sulfide