Biomedical and Biological Mass Spectrometry

Abstract

By the end of the 20th century, mass spectrometry (MS) had evolved drastically as a major analytical tool in biomedical and biological research. Recent mass spectrometers, designed for ease of handling, came into wide use in the 1990s. Soft ionization methods, which were made practical in the second half of the 1980s, allowed for the sensitive analysis of nonvolatile and thermolabile compounds by MS. Electrospray ionization (ESI) 1,2 and matrix-assisted laser desorption ionization (MALDI) 3 methods, made it possible to ionize large biomolecules and to transfer them to the gas phase, thereby becoming a valuable tool in both protein and peptide analysis [4][5][6] and in the study of drugs and their metabolites [7][8][9][10][11][12] in the human body. Many reviews of MS have recently been published, [13][14][15][16][17][18][19] and in particular, the number of reviews describing biochemical, biological, and biomedical MS have increased dramatically over the last ten years. Initially, there were many commentary reviews on new techniques, such as soft ionization methods and mass analyzers, 13-15 and more recently, review articles have focused on the biological and biomedical applications of MS. 18-21 Above all, two major fields, drug discovery and proteomics, have made marked advances based on MS.Articles in the MEDLINE database were searched, and the results are illustrated in Fig. 1 and Table 1. Over the last 15 years, a total of 79220 MS articles were placed in the database, with a 2.5-fold increase from 1987 to 1999. The number of articles using fast atom bombardment (FAB) as an ionization method remained almost constant during this period. This ionization method is a practical soft ionization procedure, which was applied to the analysis of peptides [22][23][24][25][26][27][28][29][30][31] and endogenous biological substances [32][33][34][35] in the 1980s. Atmospheric pressure chemical ionization (APCI) is a suitable method 36 for the ionization of middle or weakly polar low-molecular-weight molecules, and can be easily coupled to conventional highperformance liquid chromatography (HPLC), used at a flow rate of around 1 mL/min. [37][38][39][40][41][42][43][44][45][46][47][48] However, the number of articles concerning APCI have increased slowly, because most drugs developed recently contain polar groups which can be ionized without difficulty by the ESI technique. Japan This review focuses on biological and biomedical mass spectrometry, and covers a selection of publications in this area included in the MEDLINE database for the period 1987 -2001. Over the last 15 years, biological and biomedical mass spectrometry has progressed out of all recognition. The development of soft ionization methods, such as electrospray ionization and matrix-assisted laser desorption ionization, has mainly contributed to the remarkable progress, because they can easily produce gas-phase ions of large, polar, and thermally labile biomolecules, such as proteins, peptides, nucleic acids and others. The innovations of ionization meth...

Capillary electrophoresis – mass spectrometry: 15 years of developments and applications

“…The MS systems used include magnetic sector [8], quadrupole, ion trap [9], time of flight (TOF) [10,11], and the very powerful Fourier transform ion cyclotron (FTICR) [12][13][14][15][16][17]. More information on biomedical and biological use of MS can be found by the readers in the review of Mano and Goto [18]. Several articles on CE-MS could be found using specific ionization systems such as continuous flow fast atom bombardment [19,20], laser vaporization ionization using UV laser [21] or sonic spray ionization [22].…”

Feasibility of nonvolatile buffers in capillary electrophoresis‐electrospray ionization‐mass spectrometry of proteins

“…Mass spectrometry (MS) nowadays is an important and powerful tool for the analysis and characterization of proteins [18,19]. The multiple charging of proteins observed in electrospray ionization (ESI) allows their analysis on MS instruments with mass ranges far below the molecular masses of the proteins.…”

New Principle of Magnetophoretic Velocity Mass Analysis

“…These methods have made it possible to detect macromolecules of larger than 100 kDa by the multi-charge mode. 4 However, the ionization efficiency has still room to be improved to measure much larger proteins and DNA.The present study proposes an innovative mass analysis method by using magnetophoretic force 5 as a migrating force on a sample particle in a gas phase or low vacuo. All compounds have their own magnetic susceptibilities.…”

“…These methods have made it possible to detect macromolecules of larger than 100 kDa by the multi-charge mode. 4 However, the ionization efficiency has still room to be improved to measure much larger proteins and DNA.…”