Ion-Based Proteome-Integrated Solubility Alteration Assays for Systemwide Profiling of Protein-Molecule Interactions.
Journal
Analytical chemistry
ISSN: 1520-6882
Titre abrégé: Anal Chem
Pays: United States
ID NLM: 0370536
Informations de publication
Date de publication:
17 05 2022
17 05 2022
Historique:
pubmed:
5
5
2022
medline:
20
5
2022
entrez:
4
5
2022
Statut:
ppublish
Résumé
Unbiased drug target engagement deconvolution and mechanism of action elucidation are major challenges in drug development. Modification-free target engagement methods, such as thermal proteome profiling, have gained increasing popularity in the last several years. However, these methods have limitations, and, in any case, new orthogonal approaches are needed. Here, we present a novel isothermal method for comprehensive characterization of protein solubility alterations using the effect on protein solubility of cations and anions in the Hofmeister series. We combine the ion-based protein precipitation approach with Proteome-Integrated Solubility Alteration (PISA) analysis and use this I-PISA assay to delineate the targets of several anticancer drugs both in cell lysates and intact cells. Finally, we demonstrate that I-PISA can detect solubility changes in minute amounts of sample, opening chemical proteomics applications to small and rare biological material.
Identifiants
pubmed: 35506705
doi: 10.1021/acs.analchem.2c00391
pmc: PMC9118197
doi:
Substances chimiques
Proteome
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7066-7074Références
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