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Hsp90-Targeted Library

13,000 Compounds

The Core Strategy

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

►Analyze the structures of HSP90 and HSP70proteins 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. 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 cell stress.
The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF).

Medicinal and Computational Chemistry Dept., ChemDiv, Inc.
12760 High Bluff Dr, San Diego, CA, 92130
Phone: + 1 916 234 0888
Fax: +1 858 794 4931
Email: ChemDiv@chemdiv.com

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