Mass Spectrometry-Based Platforms for Protein Lipoxidation Profiling.

Autor: Tang Z; National Key Laboratory of Green Pesticide, College of Chemistry, Central China Normal University, Wuhan, Hubei, 430079, China., Wang T; National Key Laboratory of Green Pesticide, College of Chemistry, Central China Normal University, Wuhan, Hubei, 430079, China., Liu C; National Key Laboratory of Green Pesticide, College of Chemistry, Central China Normal University, Wuhan, Hubei, 430079, China.
Jazyk: angličtina
Zdroj: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2024 Dec 23; Vol. 30 (72), pp. e202402062. Date of Electronic Publication: 2024 Nov 09.
DOI: 10.1002/chem.202402062
Abstrakt: Lipid peroxidation, occurring through enzymatic or non-enzymatic processes, generates lipid-derived electrophiles (LDEs), which can covalently modify nucleophilic amino acid residues in proteins, a process known as protein lipoxidation. This modification can alter protein structure and function, either causing damage or regulating signalling pathways. Identifying the protein targets and specific lipoxidation sites provide important clues for unveiling the oxidative stress-related protein interaction network and molecular mechanisms of related diseases. In this review, we present a detailed overview of recent advances in protein LDE modification profiling, with a focus on mass spectrometry (MS)-based chemoproteomic platforms for global protein lipoxidation profiling.
(© 2024 Wiley-VCH GmbH.)
Databáze: MEDLINE
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