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Identification of Isoform-Selective Ligands for the Middle Domain of Heat Shock Protein 90 (Hsp90)

The molecular chaperone heat shock protein 90 (Hsp90) is a current inhibition target for the treatment of diseases, including cancer. In humans, there are two major cytosolic isoforms of Hsp90 (Hsp90α and Hsp90β). Hsp90α is inducible and Hsp90β is constitutively expressed. Most Hsp90 inhibitors are...

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Detalles Bibliográficos
Autores principales: Mak, Oi Wei, Chand, Raina, Reynisson, Jóhannes, Leung, Ivanhoe K. H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6862331/
https://www.ncbi.nlm.nih.gov/pubmed/31717777
http://dx.doi.org/10.3390/ijms20215333
Descripción
Sumario:The molecular chaperone heat shock protein 90 (Hsp90) is a current inhibition target for the treatment of diseases, including cancer. In humans, there are two major cytosolic isoforms of Hsp90 (Hsp90α and Hsp90β). Hsp90α is inducible and Hsp90β is constitutively expressed. Most Hsp90 inhibitors are pan-inhibitors that target both cytosolic isoforms of Hsp90. The development of isoform-selective inhibitors of Hsp90 may enable better clinical outcomes. Herein, by using virtual screening and binding studies, we report our work in the identification and characterisation of novel isoform-selective ligands for the middle domain of Hsp90β. Our results pave the way for further development of isoform-selective Hsp90 inhibitors.