Herein, we describe the synthesis and structure–activity relationships of cyclic peptides
designed to target heat shock protein 90 (Hsp90). Generating 19 compounds and evaluating …

Sixteen linear and cyclic peptides were designed de novo to target the C-terminus of heat
shock protein 90 (Hsp90). Protein binding data indicates that three compounds directly block …

The inhibition of the C-terminal domain of heat shock protein 90 (Hsp90) is emerging as a
novel strategy for cancer therapy, therefore the identification of a new class of C-terminal …

BACKGROUND While there is compelling rationale to use heat shock protein 90 (Hsp90)
inhibitors for treatment of advanced prostate cancer, agents that target the N‐terminal ATP …

The phenotypes produced when cells are treated with the heat shock protein 90 (Hsp90)
inhibitors AUY922 or 17‐AAG (classical inhibitors) are different to those produced when …

Macrocycles have several advantages over small‐molecule drugs when it comes to
addressing specific protein–protein interactions as therapeutic targets. Herein we report the …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone (90 kDa) that functions as
a dimer. This protein facilitates the folding, assembly, and stabilization of more than 400 …

LB76 is a cyclic peptide that shows great promise as a selective heat shock protein 90
(Hsp90) inhibitor. However despite strong binding to and inhibition of Hsp90 in cell lysate its …

2.1 Introduction: Receptor Allosterism allosteric molecules are fundamentally different from
molecules that bind to the natural receptor binding pocket for endogenous hormones and …

Classical Hsp90 inhibitors target the N-terminal ATP binding site. While these inhibitors
have had some clinical success, treatment with these molecules leads to a dramatic …