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Applications of Tandem Mass Spectrometry (MS/MS) in Protein Analysis for Biomedical Research
Summary
This review covers how tandem mass spectrometry is used to analyze proteins and peptides in biomedical research, including identifying protein sequences and modifications. The technology enables researchers to detect disease biomarkers and understand protein changes relevant to diagnostics and therapy. While not directly related to microplastics, these analytical methods are part of the broader toolkit used in environmental and health research.
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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