Applications of Tandem Mass Spectrometry (MS/MS) in Protein Analysis for Biomedical Research.
Anca-Narcisa NeaguMadhuri JayathirthaEmma BaxterMary DonnellyBrîndușa Alina PetreCostel C DariePublished in: Molecules (Basel, Switzerland) (2022)
Mass Spectrometry (MS) allows the analysis of proteins and peptides through a variety of methods, such as Electrospray Ionization-Mass Spectrometry (ESI-MS) or Matrix-Assisted Laser Desorption Ionization-Mass Spectrometry (MALDI-MS). These methods allow identification of the mass of a protein or a peptide as intact molecules or the identification of a protein through peptide-mass fingerprinting generated upon enzymatic digestion. Tandem mass spectrometry (MS/MS) allows the fragmentation of proteins and peptides to determine the amino acid sequence of proteins (top-down and middle-down proteomics) and peptides (bottom-up proteomics). Furthermore, tandem mass spectrometry also allows the identification of post-translational modifications (PTMs) of proteins and peptides. Here, we discuss the application of MS/MS in biomedical research, indicating specific examples for the identification of proteins or peptides and their PTMs as relevant biomarkers for diagnostic and therapy.
Keyphrases
- mass spectrometry
- liquid chromatography
- tandem mass spectrometry
- amino acid
- high performance liquid chromatography
- ultra high performance liquid chromatography
- ms ms
- gas chromatography
- high resolution mass spectrometry
- simultaneous determination
- high resolution
- solid phase extraction
- capillary electrophoresis
- liquid chromatography tandem mass spectrometry
- multiple sclerosis
- nitric oxide
- protein protein
- stem cells
- hydrogen peroxide
- mesenchymal stem cells