背景介绍 NVP-BEP800 binds to the N-terminal ATP-binding pocket of Hsp90. Hsp90 is a ubiquitously expressed molecular chaperone with ATPase activity involved in the conformational maturation and stability of key signaling molecules involved in cell proliferation, survival, and transformation. In BT-474 cells and A375 cells, NVP-BEP800 causes the Hsp90-p23 dissociation and client protein degradation (ErbB2) as well as the reduction of client protein phosphorylation (phospho-Akt). Degradation of these oncogenic client proteins results in tumor cell growth arrest and death. 产品介绍 NVP-BEP800 is a novel, fully synthetic, orally bioavailable inhibitor that binds to the NH(2)-terminal ATP-binding pocket of Hsp90. NVP-BEP800 (also known as VER-82576) is a novel ATP-competitive HSP90β inhibitor that binds to the NH(2)-terminal ATP-binding pocket of Heat shock protein 90 (Hsp90). NVP-BEP800 induced robust antitumor responses in tumor xenograft models, including regression in the BT-474 breast cancer model. NVP-BEP800 can radiosensitise tumour cell lines of different entities through destabilisation and depletion of several Hsp90 client proteins, thus causing the depletion of S phase and G2/M arrest, increased DNA damage and repair protraction and, to some extent, apoptosis.