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  • 03월 10일 13시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제105회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Hsp90 chaperone machinery in cancer and immunity

2010년 3월 27일 13시 14분 34초
금13C6심 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
금 11시 : 50분
생명화학 - 단백질 과학의 생화학적 접근
저자 및
서울대학교 화학생물공학부, Korea
Hsp90 is one of the most abundant molecular chaperones in eukaryotic cells, playing an important role in folding, stabilization, activation, and assembly of metastable ‘client’ proteins which include many oncogenic proteins. Inhibition of Hsp90 leads to simultaneous degradation of the oncogenic client proteins, placing Hsp90 as a promising new target for anti-cancer drug development. To identify novel classes of Hsp90 inhibitors, we utilized structure-based virtual screening of a chemical database with docking simulations in the N-terminal ATP-binding site of Hsp90, in vitro ATPase assay of yeast Hsp90, and cell-based Her2 degradation assay in a consecutive manner. As a result, we identified Hsp90 inhibitors with noble scaffolds which exert anti-proliferative effect on MCF-7 breast cancer cells. We also developed a novel tool to detect interaction between Hsp90 and Hsp90 inhibitors based on carboxylated polypyrrole nanotube (CPNT) field-effect transistor (FET) platform. The resulting platform allowed sensitive and specific detection of Hsp90 inhibitor binding to Hsp90 in real-time. Accumulating evidence suggests that Hsp90 is also involved in innate immune response by regulating various signaling molecules including NLRs (Nod-like receptors). We will discuss the biochemical analyses of a novel Hsp90 chaperone complex containing two co-chaperones, Chp-1 and of protein phosphatase 5 (PP5), which is a potential regulator of NLRs.