Kinetic Analysis of Estrogen Receptor/Ligand Interactions

Surface plasmon resonance biosensor technology was used to directly measure the binding interactions of small molecules to the ligand-binding domain of human estrogen receptor. In a screening mode, specific ligands of the receptor were easily discerned from nonligands. In a high-resolution mode, the...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 99; no. 13; pp. 8562 - 8567
Main Authors Rich, Rebecca L., Hoth, Lise R., Geoghegan, Kieran F., Brown, Thomas A., LeMotte, Peter K., Simons, Samuel P., Hensley, Preston, Myszka, David G.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 25.06.2002
National Acad Sciences
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Abstract Surface plasmon resonance biosensor technology was used to directly measure the binding interactions of small molecules to the ligand-binding domain of human estrogen receptor. In a screening mode, specific ligands of the receptor were easily discerned from nonligands. In a high-resolution mode, the association and dissociation phase binding responses were shown to be reproducible and could be fit globally to a simple interaction model to extract reaction rate constants. On average, antagonist ligands (such as tamoxifen and nafoxidine) were observed to bind to the receptor with association rates that were 500-fold slower than agonists (such as estriol and β-estradiol). This finding is consistent with these antagonists binding to an altered conformation of the receptor. The biosensor assay also could identify subtle differences in how the same ligand interacted with two different isoforms of the receptor (α and β). The biosensor's ability to determine kinetic rate constants for small molecule/protein interactions provides unique opportunities to understand the mechanisms associated with complex formation as well as new information to drive the optimization of drug candidates.
AbstractList Surface plasmon resonance biosensor technology was used to directly measure the binding interactions of small molecules to the ligand-binding domain of human estrogen receptor. In a screening mode, specific ligands of the receptor were easily discerned from nonligands. In a high-resolution mode, the association and dissociation phase binding responses were shown to be reproducible and could be fit globally to a simple interaction model to extract reaction rate constants. On average, antagonist ligands (such as tamoxifen and nafoxidine) were observed to bind to the receptor with association rates that were 500-fold slower than agonists (such as estriol and β-estradiol). This finding is consistent with these antagonists binding to an altered conformation of the receptor. The biosensor assay also could identify subtle differences in how the same ligand interacted with two different isoforms of the receptor (α and β). The biosensor's ability to determine kinetic rate constants for small molecule/protein interactions provides unique opportunities to understand the mechanisms associated with complex formation as well as new information to drive the optimization of drug candidates.
Surface plasmon resonance biosensor technology was used to directly measure the binding interactions of small molecules to the ligand-binding domain of human estrogen receptor. In a screening mode, specific ligands of the receptor were easily discerned from nonligands. In a high-resolution mode, the association and dissociation phase binding responses were shown to be reproducible and could be fit globally to a simple interaction model to extract reaction rate constants. On average, antagonist ligands (such as tamoxifen and nafoxidine) were observed to bind to the receptor with association rates that were 500-fold slower than agonists (such as estriol and beta-estradiol). This finding is consistent with these antagonists binding to an altered conformation of the receptor. The biosensor assay also could identify subtle differences in how the same ligand interacted with two different isoforms of the receptor (alpha and beta). The biosensor's ability to determine kinetic rate constants for small molecule/protein interactions provides unique opportunities to understand the mechanisms associated with complex formation as well as new information to drive the optimization of drug candidates.
Surface plasmon resonance biosensor technology was used to directly measure the binding interactions of small molecules to the ligand-binding domain of human estrogen receptor. In a screening mode, specific ligands of the receptor were easily discerned from noligands.
Author Geoghegan, Kieran F.
Rich, Rebecca L.
Simons, Samuel P.
Hoth, Lise R.
LeMotte, Peter K.
Hensley, Preston
Myszka, David G.
Brown, Thomas A.
AuthorAffiliation Center for Biomolecular Interaction Analysis, University of Utah, Salt Lake City, UT 84132; and † Pfizer Global Research and Development, Eastern Point Road, Groton, CT 06340
AuthorAffiliation_xml – name: Center for Biomolecular Interaction Analysis, University of Utah, Salt Lake City, UT 84132; and † Pfizer Global Research and Development, Eastern Point Road, Groton, CT 06340
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  givenname: Lise R.
  surname: Hoth
  fullname: Hoth, Lise R.
– sequence: 3
  givenname: Kieran F.
  surname: Geoghegan
  fullname: Geoghegan, Kieran F.
– sequence: 4
  givenname: Thomas A.
  surname: Brown
  fullname: Brown, Thomas A.
– sequence: 5
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  surname: LeMotte
  fullname: LeMotte, Peter K.
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  surname: Myszka
  fullname: Myszka, David G.
BackLink https://www.ncbi.nlm.nih.gov/pubmed/12077320$$D View this record in MEDLINE/PubMed
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Communicated by Pamela J. Bjorkman, California Institute of Technology, Pasadena, CA
To whom reprint requests should be addressed at: Center for Biomolecular Interaction Analysis, School of Medicine 4A417, 50 North Medical Drive, Salt Lake City, UT. E-mail: dmyszka@cores.utah.edu.
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Snippet Surface plasmon resonance biosensor technology was used to directly measure the binding interactions of small molecules to the ligand-binding domain of human...
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SubjectTerms Agonists
Analysis
Antibodies
Antibodies, Monoclonal - metabolism
Benzhydryl Compounds
Biochemistry
Biological Sciences
Biosensing techniques
Bisphenols
Dehydroepiandrosterone - metabolism
Drug interactions
Estrogen Receptor alpha
Estrogen Receptor beta
Estrogens
Kinetics
Ligands
Phenols - metabolism
Protein isoforms
Receptors
Receptors, Estrogen - chemistry
Receptors, Estrogen - metabolism
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Title Kinetic Analysis of Estrogen Receptor/Ligand Interactions
URI https://www.jstor.org/stable/3059055
http://www.pnas.org/content/99/13/8562.abstract
https://www.ncbi.nlm.nih.gov/pubmed/12077320
https://www.proquest.com/docview/201392177
https://search.proquest.com/docview/18413620
https://search.proquest.com/docview/71862922
https://pubmed.ncbi.nlm.nih.gov/PMC124311
Volume 99
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