title: Identification of small molecules affecting p53-MDM2/MDMX interaction by fluorescence polarization.
abstract: Fluorescence polarization (FP) has become a powerful technique to quantitatively analyze the binding of a small soluble fluorescence-labeled probe to a larger soluble protein and its displacement by other molecules. Here, we describe a detailed protocol to identify small molecules capable of targeting p53-MDM2/MDMX interactions using a fluorescence polarization assay with Rhodamine-labeled p53 peptides.
authors.affiliation: Department of Biochemistry & Molecular Biology and Tulane Cancer Center, Tulane University School of Medicine, New Orleans, LA, USA.
authors.forename: Qi
authors.initials: Q
authors.lastname: Zhang
authors.forename: Hua
authors.initials: H
authors.lastname: Lu
mesh_terms: D018797:Cell Cycle Proteins; D005454:Fluorescence Polarization / Q000379:methods*; D015870:Gene Expression; D006801:Humans; D009687:Nuclear Proteins / Q000737:chemistry* / Q000235:genetics; D011485:Protein Binding; D011518:Proto-Oncogene Proteins / Q000737:chemistry* / Q000235:genetics; D051736:Proto-Oncogene Proteins c-mdm2 / Q000737:chemistry* / Q000235:genetics; D015203:Reproducibility of Results; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000235:genetics
chemical_list: D018797:Cell Cycle Proteins; C482775:MDM4 protein, human; D009687:Nuclear Proteins; D011518:Proto-Oncogene Proteins; D016159:Tumor Suppressor Protein p53; C497206:MDM2 protein, human; D051736:Proto-Oncogene Proteins c-mdm2