Conjugation of primary amine groups in targeted proteomics.

Autor: Cai Y; Department of Chemistry, University of New Orleans, New Orleans, Louisiana, USA.
Jazyk: angličtina
Zdroj: Mass spectrometry reviews [Mass Spectrom Rev] 2024 Sep 04. Date of Electronic Publication: 2024 Sep 04.
DOI: 10.1002/mas.21906
Abstrakt: Primary amines, in the form of unmodified N-terminus of peptide/protein and unmodified lysine residue, are perhaps the most important functional groups that can serve as the starting points in proteomic analysis, especially via mass spectrometry-based approaches. A variety of multifunctional probes that conjugate primary amine groups through covalent bonds have been developed and employed to facilitate protein/protein complex characterization, including identification, quantification, structure and localization elucidation, protein-protein interaction investigation, and so forth. As an integral part of more accurate peptide quantification in targeted proteomics, isobaric stable isotope-coded primary amine labeling approaches eventually facilitated protein/peptide characterization at the single-cell level, paving the way for single-cell proteomics. The development and advances in the field can be reviewed in terms of key components of a multifunctional probe: functional groups and chemistry for primary amine conjugation; hetero-bifunctional moiety for separation/enrichment of conjugated protein/protein complex; and functionalized linker/spacer. Perspectives are primarily focused on optimizing primary amine conjugation under physiological conditions to improve characterization of native proteins, especially those associated with the surface of living cells/microorganisms.
(© 2024 Wiley Periodicals LLC.)
Databáze: MEDLINE
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