A library of noviosylated coumarin analogues.
The DNA gyrase inhibitor, novobiocin, was recently shown to inhibit Hsp90 via a previously unrecognized C-terminal ATP-binding site. Previous structure-activity relationship studies identified key moieties that appear important for Hsp90 inhibitory activity. In an effort to provide a more efficacious lead compound, a parallel library of noviosylated coumarin analogues was prepared.
Huang
Yung-Tzung
YT
Department of Medicinal Chemistry and The Center for Chemical Methodologies and Library Development, The University of Kansas, 1251 Wescoe Hall Drive, Malott Hall 4070, Lawrence, Kansas 66045-7563, USA.
Blagg
Brian S J
BS
D001897:Boronic Acids / Q000737:chemistry; D003374:Coumarins / Q000138:chemical synthesis / Q000737:chemistry*; D016208:Databases, Factual; D004951:Esterification; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D007463:Iodobenzoates / Q000138:chemical synthesis / Q000737:chemistry; D015394:Molecular Structure; D009675:Novobiocin / Q000737:chemistry* / Q000494:pharmacology; D013329:Structure-Activity Relationship
D001897:Boronic Acids; D003374:Coumarins; D018841:HSP90 Heat-Shock Proteins; D007463:Iodobenzoates; D009675:Novobiocin; C030123:coumarin