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Resorcinol-Based Grp94-Selective Inhibitors.

Anuj Khandelwal¹, Vincent M Crowley¹, Brian S J Blagg²

¹Department of Medicinal Chemistry, The University of Kansas, 1251 Wescoe Hall Drive, Malott Hall 4070, Lawrence, Kansas 66045, United States.

ACS Medicinal Chemistry Letters

|October 24, 2017

Summary

This summary is machine-generated.

Researchers developed a novel inhibitor targeting Glucose-regulated protein 94 (Grp94), a key protein in cancer. This selective Grp94 inhibitor shows promise for treating diseases like multiple myeloma.

Keywords:

Grp94 Heat shock protein 90 cancer multiple myeloma

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Area of Science:

Biochemistry
Molecular Biology
Drug Discovery

Background:

Glucose-regulated protein 94 (Grp94) is an endoplasmic reticulum chaperone and a member of the Hsp90 protein family.
Grp94's unique structural features, including a five amino acid insertion, create exclusive binding pockets for targeted inhibition.
It is recognized as a potential therapeutic target for various diseases.

Purpose of the Study:

To develop and characterize the first resorcinol-based inhibitor selective for Grp94.
To evaluate the inhibitor's affinity, selectivity, and efficacy against cancer cells.

Main Methods:

Structure-based drug design utilizing Grp94's unique hydrophobic S2 subpocket.
Biochemical assays to determine inhibitor affinity and selectivity.
Cell-based assays to assess cytotoxic effects on multiple myeloma cells.

Main Results:

Development of a Grp94-selective inhibitor with low nanomolar affinity.
Demonstrated approximately 10-fold selectivity for Grp94 over other Hsp90 family members.
Achieved low micromolar GI50 values against multiple myeloma cell lines.

Conclusions:

The novel resorcinol-based compound is the first selective Grp94 inhibitor.
These findings validate Grp94 as a promising therapeutic target for multiple myeloma.
Selective inhibition of Grp94 represents a viable strategy for cancer treatment.