Thermal proteome profiling: a technique for a comprehensive assessment of protein status.

Author: Yanhua QIU ¹ ; Bintao ZHAI ¹ ; Yubin BAI ¹ ; Shulin CHEN ² ; Jiyu ZHANG ¹
Author Information

1. Lanzhou Institute of Husbandry and Pharmaceutical Sciences, Chinese Academy of Agricultural Sciences, Lanzhou 730050, Gansu, China.
2. College of Veterinary Medicine, Northwest A & F University, Yangling 712100, Shaanxi, China.
Publication Type:Journal Article
Keywords: drug targets; ligand; protein; thermal proteome profiling
MeSH: Proteome; Mass Spectrometry
From: Chinese Journal of Biotechnology 2022;38(10):3628-3637
CountryChina
Language:Chinese
Abstract: Thermal proteome profiling (TPP) is a combination of cellular thermal shift assay (CETSA) and quantitative mass spectrometry (MS), also termed as MS-CETSA. TPP determines the stability of the entire proteome by measuring the content of soluble proteins in cells or cell lysates at different heating temperatures. Proteins can change their thermostability when interacting with small molecules (e.g., drugs or metabolites), nucleic acids, or other proteins or posttranslational modification, while TPP can identify target proteins based on the difference in thermostability with or without ligand-binding. At present, TPP has been applied to identify the targets and off-targets of drugs and interrogate protein-metabolite and protein-protein interactions. Due to limited understanding of this technology, this review introduced the principles, methods, applications, advantages and limitations of TPP.