title: Fluoresceinated FKBP12 ligands for a high-throughput fluorescence polarization assay.
abstract: Several fluoresceinated FKBP12 ligands have been prepared for a high-throughput fluorescence polarization assay. K(i)s for FKBP12 rotamase inhibition by these ligands range from 1.3 microM to 32 nM, and their design is based on X-ray crystal structures of FKBP12 complexed with known immunophilin ligands.
authors.affiliation: Bristol-Myers Squibb Pharmaceutical Research Institute, Wallingford, CT 06492-7660, USA. gene.dubowchik@bms.com
authors.forename: G M
authors.initials: GM
authors.lastname: Dubowchik
authors.forename: J L
authors.initials: JL
authors.lastname: Ditta
authors.forename: J J
authors.initials: JJ
authors.lastname: Herbst
authors.forename: S
authors.initials: S
authors.lastname: Bollini
authors.forename: A
authors.initials: A
authors.lastname: Vinitsky
mesh_terms: D018360:Crystallography, X-Ray; D019793:Fluorescein / Q000737:chemistry; D016231:Fluorescence Polarization Immunoassay; D005456:Fluorescent Dyes / Q000138:chemical synthesis* / Q000494:pharmacology; D020104:Immunophilins / Q000737:chemistry*; D008024:Ligands; D011485:Protein Binding; D016559:Tacrolimus / Q000378:metabolism; D022021:Tacrolimus Binding Proteins
chemical_list: D005456:Fluorescent Dyes; D008024:Ligands; D022021:Tacrolimus Binding Proteins; D020104:Immunophilins; D019793:Fluorescein; D016559:Tacrolimus