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Related Experiment Video

Updated: Mar 2, 2026

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Published on: March 31, 2022

Structure-based virtual screening and optimization of modulators targeting Hsp90-Cdc37 interaction.

Lei Wang¹, Li Li¹, Zi-Han Zhou²

¹State Key Laboratory of Natural Medicines, Jiang Su Key Laboratory of Drug Design and Optimization, China Pharmaceutical University, Nanjing 210009, China; Department of Medicinal Chemistry, School of Pharmacy, China Pharmaceutical University, Nanjing 210009, China.

European Journal of Medicinal Chemistry

|May 9, 2017

Summary

Researchers identified novel small molecules targeting the Hsp90-Cdc37 protein-protein interaction (PPI). Compound 10 showed potent antiproliferative activity against cancer cells, representing a new class of Hsp90-Cdc37 PPI inhibitors.

Keywords:

Hsp90-Cdc37 Protein-protein interaction Virtual screening

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Last Updated: Mar 2, 2026

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Area of Science:

Biochemistry
Medicinal Chemistry
Oncology

Background:

Heat shock protein 90 (Hsp90) is a crucial molecular chaperone involved in cancer progression.
Targeting the Hsp90-Cdc37 protein-protein interaction (PPI) offers an alternative strategy for Hsp90 inhibition.
Developing small molecules to disrupt this specific PPI is a promising area for cancer therapy.

Purpose of the Study:

To identify and characterize novel small molecules that inhibit the Hsp90-Cdc37 PPI.
To optimize lead compounds through structure-activity relationship (SAR) analysis.
To evaluate the antiproliferative effects of identified compounds against various cancer cell lines.

Main Methods:

Structure-based virtual screening was employed to identify initial hit compounds.
Synthesis of derivative compounds based on virtual screening results.
Biological evaluation including inhibitory concentration (IC50) and binding affinity (KD) measurements.
Antiproliferative assays against MCF-7, SKBR3, and A549 cancer cell lines.

Main Results:

Virtual screening identified potential inhibitors of the Hsp90-Cdc37 complex.
Structural optimization led to the discovery of compound 10.
Compound 10 demonstrated a promising inhibitory effect (IC50 = 27 μM) and moderate binding capacity (KD = 40 μM).
Compound 10 exhibited significant antiproliferative activity against MCF-7 (IC50 = 26 μM), SKBR3 (IC50 = 15 μM), and A549 (IC50 = 38 μM) cell lines.

Conclusions:

Compound 10 is a novel, non-natural small molecule that effectively targets the Hsp90-Cdc37 PPI.
The findings provide initial evidence for targeting this specific PPI with small molecules.
Compound 10 warrants further investigation as a potential anticancer therapeutic agent.