Applications of Tandem Mass Spectrometry (MS/MS) in Protein Analysis for Biomedical Research |
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| Authors: | Anca-Narcisa Neagu Madhuri Jayathirtha Emma Baxter Mary Donnelly Brindusa Alina Petre Costel C Darie |
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| Institution: | 1.Laboratory of Animal Histology, Faculty of Biology, “Alexandru Ioan Cuza” University of Iasi, Carol I bvd. No. 22, 700505 Iasi, Romania;2.Biochemistry & Proteomics Group, Department of Chemistry and Biomolecular Science, Clarkson University, 8 Clarkson Avenue, Potsdam, NY 13699, USA; (M.J.); (E.B.); (M.D.); (B.A.P.);3.Laboratory of Biochemistry, Faculty of Chemistry, “Alexandru Ioan Cuza” University of Iasi, Carol I bvd. No. 22A, 700505 Iasi, Romania |
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| Abstract: | 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. |
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| Keywords: | proteomics tandem mass spectrometry (MS/MS) biomedical research biomarkers |
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