Streamlined analysis of drug targets by proteome integral solubility alteration indicates organ-specific engagement

Tanveer Singh Batth*, Marie Locard-Paulet, Nadezhda T. Doncheva, Blanca Lopez Mendez, Lars Juhl Jensen, Jesper Velgaard Olsen*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Proteins are the primary targets of almost all small molecule drugs. However, even the most selectively designed drugs can potentially target several unknown proteins. Identification of potential drug targets can facilitate design of new drugs and repurposing of existing ones. Current state-of-the-art proteomics methodologies enable screening of thousands of proteins against a limited number of drug molecules. Here we report the development of a label-free quantitative proteomics approach that enables proteome-wide screening of small organic molecules in a scalable, reproducible, and rapid manner by streamlining the proteome integral solubility alteration (PISA) assay. We used rat organs ex-vivo to determine organ specific targets of medical drugs and enzyme inhibitors to identify drug targets for common drugs such as Ibuprofen. Finally, global drug profiling revealed overarching trends of how small molecules affect the proteome through either direct or indirect protein interactions.

Original languageEnglish
Article number8923
JournalNature Communications
Volume15
Issue number1
Number of pages17
ISSN2041-1723
DOIs
Publication statusPublished - 2024

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© The Author(s) 2024.

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