title: Kinetic analysis of the estrogen receptor alpha using RIfS.
abstract: The label-free time-resolved reflectometric interference spectroscopy has been used to study the interaction of the human estrogen receptor alpha (ERa) and different types of ligands. Different possible sensor surface coatings including various estrogen derivatives were evaluated for their suitability for detection of ERa. The determination of the kinetic and thermodynamic constants was carried out for the interaction in the heterogeneous phase as well as for the interaction in homogeneous phase. In addition, the affinity of 11 ligands ranging from natural hormones and pharmaceuticals to endocrine disrupting chemicals (EDCs) has been determined with this label-free assay format.
authors.affiliation: Institute of Physical and Theoretical Chemistry, Eberhard-Karls-University of Tübingen, Germany. peter.fechner@ipc.uni-tuebingen.de
authors.forename: Peter
authors.initials: P
authors.lastname: Fechner
authors.forename: Florian
authors.initials: F
authors.lastname: Pröll
authors.forename: Christiane
authors.initials: C
authors.lastname: Albrecht
authors.forename: Günter
authors.initials: G
authors.lastname: Gauglitz
mesh_terms: D001665:Binding Sites; D052244:Endocrine Disruptors / Q000378:metabolism*; D047628:Estrogen Receptor alpha / Q000737:chemistry / Q000378:metabolism*; D006728:Hormones / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D013057:Spectrum Analysis / Q000379:methods; D013816:Thermodynamics
chemical_list: C506487:ESR1 protein, human; D052244:Endocrine Disruptors; D047628:Estrogen Receptor alpha; D006728:Hormones; D008024:Ligands