1.
Chem Commun (Camb)
; 52(3): 501-4, 2016 Jan 11.
Artigo
em Inglês
| MEDLINE
| ID: mdl-26528929
RESUMO
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.