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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Updated: Jun 12, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
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Stability-Based Proteomic Methods Add Value to Activity-Based Protein Profiling Studies.

You Zou1, Diego J Sanson1, Jianli Wu2

  • 1Department of Chemistry, Duke University, Durham, North Carolina 27708, United States.

ACS Chemical Biology
|June 11, 2026
PubMed
Summary
This summary is machine-generated.

Stability-based proteomics, including SPROX and TPP, effectively identifies covalent drug targets. This study revealed ALDH1A3 as a key off-target for the KRAS inhibitor ARS-1620, impacting its therapeutic efficacy.

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Area of Science:

  • Proteomics
  • Chemical Biology
  • Drug Discovery

Background:

  • Covalent inhibitors offer therapeutic benefits but need thorough profiling for on- and off-target effects.
  • Identifying off-target interactions is crucial for understanding drug mechanisms and potential toxicities.

Purpose of the Study:

  • To evaluate stability-based proteomic methods (SPROX and TPP) for identifying protein targets of covalent inhibitors.
  • To characterize the off-target interactions of the KRAS G12C inhibitor ARS-1620.

Main Methods:

  • Utilized stability of proteins from rates of oxidation (SPROX) and thermal protein profiling (TPP) on H358 cell lysates.
  • Employed mass spectrometry-based covalent site mapping and enzymatic assays.
  • Performed covalent docking and functional knockdown experiments.

Main Results:

  • Both SPROX and TPP identified KRAS as the on-target and revealed multiple off-targets.
  • Aldehyde dehydrogenase 1A3 (ALDH1A3) was identified as a reproducible off-target missed by previous methods.
  • ARS-1620 covalently binds to C314 on ALDH1A3, inhibiting its enzymatic activity and contributing to ARS-1620's cell-killing effects.

Conclusions:

  • Stability-based proteomics is a powerful strategy for covalent drug target identification.
  • ALDH1A3 plays a significant role in the mode of action of ARS-1620.
  • This study expands the understanding of ARS-1620's biological activity and off-target profile.