title: The first report of direct inhibitors that target the C-terminal MEEVD region on heat shock protein 90.
abstract: Sixteen linear and cyclic peptides were designed de novo to target the C-terminus of heat shock protein 90 (Hsp90). Protein binding data indicates that three compounds directly block co-chaperone access to Hsp90's C-terminus and luciferase renaturation assays confirm Hsp90-mediated protein folding is disrupted. This is the first report of an inhibitor that binds directly to the C-terminal MEEVD region of Hsp90.
authors.affiliation: School of Chemistry, Gate 2 High Street, Dalton 219, University of New South Wales, Sydney, Australia. s.mcalpine@unsw.edu.au.
authors.forename: L K
authors.initials: LK
authors.lastname: Buckton
authors.forename: H
authors.initials: H
authors.lastname: Wahyudi
authors.forename: S R
authors.initials: SR
authors.lastname: McAlpine
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D016503:Drug Delivery Systems; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors*; D020128:Inhibitory Concentration 50; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D018841:HSP90 Heat-Shock Proteins