Thermal proteome profiling for interrogating protein interactions.
drug discovery
metabolites
protein complexes
proteomics
thermal proteome profiling
Journal
Molecular systems biology
ISSN: 1744-4292
Titre abrégé: Mol Syst Biol
Pays: England
ID NLM: 101235389
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
13
09
2019
revised:
15
01
2020
accepted:
27
01
2020
entrez:
6
3
2020
pubmed:
7
3
2020
medline:
4
2
2021
Statut:
ppublish
Résumé
Thermal proteome profiling (TPP) is based on the principle that, when subjected to heat, proteins denature and become insoluble. Proteins can change their thermal stability upon interactions with small molecules (such as drugs or metabolites), nucleic acids or other proteins, or upon post-translational modifications. TPP uses multiplexed quantitative mass spectrometry-based proteomics to monitor the melting profile of thousands of expressed proteins. Importantly, this approach can be performed in vitro, in situ, or in vivo. It has been successfully applied to identify targets and off-targets of drugs, or to study protein-metabolite and protein-protein interactions. Therefore, TPP provides a unique insight into protein state and interactions in their native context and at a proteome-wide level, allowing to study basic biological processes and their underlying mechanisms.
Identifiants
pubmed: 32133759
doi: 10.15252/msb.20199232
pmc: PMC7057112
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e9232Informations de copyright
© 2020 The Authors. Published under the terms of the CC BY 4.0 license.
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