Use of a real-time fluorescence monitoring system for high-throughput screening for prolyl isomerase inhibitors.
Cyclophilin is a ubiquitous peptidyl prolyl cis/trans isomerase that plays critical roles in many biological processes. A number of cyclophilin inhibitors have been designed based on the structure of the immunosuppressant cyclosporin A. To discover inhibitors that have other structures, the authors established the high-throughput screening (HTS) method using FDSS6000 real-time fluorescence detector. The inhibitors identified with this HTS showed significant correlation with direct interaction as measured by surface plasmon resonance. This high-throughput assay system is a powerful tool for the discovery of peptidylprolyl isomerase inhibitors.
Mori
Tadashi
T
Molecular Enzymology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Itami
Seima
S
Yanagi
Tomotaka
T
Tatara
Yota
Y
Takamiya
Mari
M
Uchida
Takafumi
T
D021983:Cyclophilins / Q000037:antagonists & inhibitors; D004791:Enzyme Inhibitors / Q000032:analysis* / Q000494:pharmacology*; D005470:Fluorometry / Q000379:methods*; D007700:Kinetics; D019696:Peptidylprolyl Isomerase / Q000037:antagonists & inhibitors*; D015203:Reproducibility of Results; D054852:Small Molecule Libraries / Q000032:analysis / Q000494:pharmacology; D020349:Surface Plasmon Resonance; D013997:Time Factors
D004791:Enzyme Inhibitors; D054852:Small Molecule Libraries; D021983:Cyclophilins; D019696:Peptidylprolyl Isomerase