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Updated: May 21, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Reengineering Protease Inhibitors to Disrupt Hsp70 Chaperone Function.

Aweon Richards¹, Ascensión Ariza-Mateos², Antara Ghosh¹

¹Department of Chemistry, New York University, New York, USA.

Angewandte Chemie (International Ed. in English)

|May 19, 2026

Summary

This summary is machine-generated.

Researchers repurposed protease inhibitor scaffolds to disrupt bacterial Hsp70 (DnaK) function. This approach offers a novel strategy for developing new antibacterial agents targeting essential heat shock protein 70 chaperones.

Keywords:

DnaK allosteric inhibition molecular chaperones peptidomimetics proteotoxic stress

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Last Updated: May 21, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

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Published on: January 20, 2023

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Purification of Hsp104, a Protein Disaggregase

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

Area of Science:

Biochemistry
Molecular Biology
Drug Discovery

Background:

Heat shock protein 70 (Hsp70) chaperones are crucial for protein homeostasis.
Bacterial Hsp70, DnaK, is a potential antibacterial target due to its roles in growth and stress response.
Targeting Hsp70s across species with small molecules is challenging.

Purpose of the Study:

To investigate the interaction of protease inhibitor scaffolds with bacterial DnaK.
To design novel peptidomimetics for inhibiting Hsp70 chaperone activity.
To explore generalizable methods for targeting Hsp70s.

Main Methods:

Structure-function studies of telaprevir analogs against bacterial DnaK.
X-ray crystallography to analyze co-complexes of DnaK with inhibitors.
Synthesis of unnatural peptide sequences based on structural insights.

Main Results:

Peptidomimetic scaffolds, originally designed for protease inhibition, bind to bacterial DnaK.
Structural analysis revealed specific ligand-protein interactions within DnaK's substrate binding domain.
Designed peptidomimetics demonstrated varying inhibitory potencies against DnaK.
Shortened peptidomimetics were synthesized to allosterically inhibit DnaK's ATPase activity.

Conclusions:

Protease inhibitor scaffolds can be adapted to inhibit Hsp70 chaperone function.
This study provides a foundation for developing novel antibacterial agents targeting bacterial Hsp70.
The findings offer a generalizable strategy for modulating Hsp70 activity across different species.