Photoaffinity labeling coupled to MS to identify peptide biological partners: Secondary reactions, for better or for worse?

Autor: Walrant A; Laboratoire des Biomolécules, LBM, Sorbonne Université, École normale supérieure, PSL University, CNRS, Paris, France., Sachon E; Laboratoire des Biomolécules, LBM, Sorbonne Université, École normale supérieure, PSL University, CNRS, Paris, France.; Sorbonne Université, Mass Spectrometry Sciences Sorbonne Université, MS3U platform, Fédération de Chimie moléculaire de Paris centre, Paris, France.
Jazyk: angličtina
Zdroj: Mass spectrometry reviews [Mass Spectrom Rev] 2024 Apr 05. Date of Electronic Publication: 2024 Apr 05.
DOI: 10.1002/mas.21880
Abstrakt: Affinity photolabeling is a smart method to study noncovalent and transient interactions and provide a submolecular picture of the contacts between interacting partners. In this review, we will focus on the identification of peptide partners using photoaffinity labeling coupled to mass spectrometry in different contexts such as in vitro with a purified potential partner, in model systems such as model membranes, and with live cells using both targeted and nontargeted proteomics studies. Different biological partners will be described, among which glycoconjugates, oligonucleotides, peptides, proteins, and lipids, with the photoreactive label inserted either on the peptide of interest or on the potential partner. Particular attention will be paid to the observation and characterization of specific rearrangements following the photolabeling reaction, which can help characterize photoadducts and provide a better understanding of the interacting systems and environment.
(© 2024 The Authors. Mass Spectrometry Reviews published by John Wiley & Sons Ltd.)
Databáze: MEDLINE
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