Optimization of triazole-based small molecule disruptors of the Aha1/Hsp90 complex that manifest potent activities

Recent structure-activity relationship (SAR) studies identified multiple Hsp90/Aha1 small molecule disruptors that manifest moderately improved potencies and physiochemical properties. Among these molecules, a 1,5-bisubstituted-1,2,3-triazole containing molecule (Triazole A), demonstrated the importance of a cis-amide bond. Consequently, this work aimed to optimize Triazole A via a nitrogen scan and Topliss tree approach. The potency was determined against cell lysates and co-Immunoprecipitation (co-IP) experiments. The most efficacious molecules were evaluated for physiochemical properties that include aqueous solubility, human liver microsome half-life, and MDCK-MDR1 permeability. New molecules emerged from this study that manifest nanomolar potency and improved activity in cell-based co-IP experiments. These new molecules represent a significant improvement over prior Hsp90/Aha1 disruptors and provide chemical tools to investigate the significance of Hsp90/Aha1 complexes.

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Publication Details

Journal
European Journal of Medicinal Chemistry
Published
2026-02-03
DOI
https://doi.org/10.1016/j.ejmech.2026.118612
Primary Topic
Heat shock proteins research
Type
article
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article

Optimization of triazole-based small molecule disruptors of the Aha1/Hsp90 complex that manifest potent activities

Kevin Catalfano, Margaret H. Rakonick, Brian S.J. Blagg
European Journal of Medicinal Chemistry
Heat shock proteins research
article

Optimization of triazole-based small molecule disruptors of the Aha1/Hsp90 complex that manifest potent activities

Kevin Catalfano, Margaret H. Rakonick, Brian S.J. Blagg
article en

Abstract

Recent structure-activity relationship (SAR) studies identified multiple Hsp90/Aha1 small molecule disruptors that manifest moderately improved potencies and physiochemical properties. Among these molecules, a 1,5-bisubstituted-1,2,3-triazole containing molecule (Triazole A), demonstrated the importance of a cis-amide bond. Consequently, this work aimed to optimize Triazole A via a nitrogen scan and Topliss tree approach. The potency was determined against cell lysates and co-Immunoprecipitation (co-IP) experiments. The most efficacious molecules were evaluated for physiochemical properties that include aqueous solubility, human liver microsome half-life, and MDCK-MDR1 permeability. New molecules emerged from this study that manifest nanomolar potency and improved activity in cell-based co-IP experiments. These new molecules represent a significant improvement over prior Hsp90/Aha1 disruptors and provide chemical tools to investigate the significance of Hsp90/Aha1 complexes.

European Journal of Medicinal ChemistryVol. 308
University of Notre Dame (US)
Openalex Percentile: Top 70%
Heat shock proteins research
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Optimization of triazole-based small molecule disruptors of the Aha1/Hsp90 complex that manifest potent activities — Kevin Catalfano, Margaret H. Rakonick, et al. · European Journal of Medicinal Chemistry (2026) | TGRS Research Map | TGRS