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Hsp90-Targeted Library

Preferred format:
Desirable size of the custom library selection:
  • Mg
  • uMol
The Core Strategy

Analyze the structures of reported HSP90/70 inhibitors (more than 1K molecules):

►Analyze the structures of HSP90 and HSP70 proteins and conformational shifts within the active binding site observed upon ligand binding;
►Binding modes and allosteric binding sites identification/analysis;
►Include selective HSP90 and HSP70 binders;
►3D-model construction/validation;
►Select small-molecule compounds from ChemDiv store (more than 1.5 mil molecules) with potential HSP90/70 activity following several structure determinant, including similarity, privileged scaffolds and “med-chem” filters;
►Molecular Docking of selected compounds / “Pro-Drug” approach / Heat shock proteins (HSP) are a family of proteins that are produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress.
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