title: Screening for protein kinase C ligands using fluorescence resonance energy transfer.
abstract: Protein kinase C (PKC) is correlated with cell signaling pathways and also receives attention as a therapeutic target for cancer and Alzheimer-type dementia. The application of Förster/fluorescence resonance energy transfer (FRET) phenomena to detect binding between proteins and small molecules, for example, PKC and its ligands, underlies a fluorescence-based assay method suitable for high-throughput screening. To accelerate studies on PKC functions in processing signals using small molecules and the development of drugs that target PKC, novel methods for the assessment of the PKC binding affinity of compounds are necessary. We previously developed solvatochromic fluorophore-based methods for that assessment. In this study, a novel method for a FRET-based PKC binding assay was developed and is expected to overcome the limitations of solvatochromic fluorophores.
authors.affiliation: Department of Medicinal Chemistry, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University.
authors.forename: Nami
authors.initials: N
authors.lastname: Ohashi
authors.forename: Wataru
authors.initials: W
authors.lastname: Nomura
authors.forename: Natsuki
authors.initials: N
authors.lastname: Minato
authors.forename: Hirokazu
authors.initials: H
authors.lastname: Tamamura
mesh_terms: D019793:Fluorescein / Q000737:chemistry*; D031541:Fluorescence Resonance Energy Transfer; D057166:High-Throughput Screening Assays; D007700:Kinetics; D007783:Lactones / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D011485:Protein Binding; D011493:Protein Kinase C / Q000737:chemistry* / Q000378:metabolism; D054852:Small Molecule Libraries / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D007783:Lactones; D008024:Ligands; D054852:Small Molecule Libraries; D011493:Protein Kinase C; D019793:Fluorescein