Your cart is empty.
Hsp90-Targeted Library

Hsp90-Targeted Library

Files to download
Preferred format
Desirable size of the custom library selection
Number of compounds
Amount
Volume
uL
Description
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.
X
X
Send a message
Request a call

Your Name*

Your E-mail*

Company*

Type in your message here…*
* Required fields

By submitting this form you confirm that you have read and accepted our privacy policy. Your data will be used exclusively for this purpose.


Your Name*

Your Phone*

Company*

* Required fields

By submitting this form you confirm that you have read and accepted our privacy policy. Your data will be used exclusively for this purpose.