Applications of Tandem Mass Spectrometry (MS/MS) in Protein Analysis for Biomedical Research

Overview

Journal Molecules

Publisher MDPI

Specialty Biology

Date 2022 Apr 23

PMID 35458608

Authors

Anca-Narcisa Neagu

Madhuri Jayathirtha

Emma Baxter

Mary Donnelly

Brindusa Alina Petre

Costel C Darie

Affiliations

Soon will be listed here.

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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