De novo sequencing of proteolytic peptides by a combination of C-terminal derivatization and nano-electrospray/ collision-induced dissociation mass spectrometry

Lindh, Ingemar; Bergman, Tomas; Sjövall, Jan; Griffiths, William J.

doi:10.1016/s1044-0305(00)00138-0

Cited by 28 publications

(20 citation statements)

References 42 publications

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“…Zaia and Biemann (1995) and Zaia (1996) developed a two-step method in which the peptide is condensed with iodoacetic anhydride and reacted with trimethylamine or other higher amines to form either an N-trimethylammonium acetyl derivative or higher homologs. Other peptide modi®cations include reacting the N-terminus with (triphenylphosphonium) ethyl bromide (Sadagopan & Watson, 2000), 4-aminonaphthalenesulfonic acid (Lindh et al, 1994(Lindh et al, , 1998(Lindh et al, , 2000, or 2-hexenal (Baker, Wiesler & Novotny, 1999). Huang et al (1997), Liao and Allison (1995), and Liao, Huang and Allison (1997) introduced a simple and ef®cient method for peptide N-terminal modi®cation.…”

Section: G Peptidesmentioning

confidence: 99%

Applications and mechanisms of charge-remote fragmentation

Cheng

Gross

2000

Mass Spectrom. Rev.

255

119

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Section: G Peptidesmentioning

confidence: 99%

Applications and mechanisms of charge-remote fragmentation

Cheng

Gross

2000

Mass Spectrom. Rev.

255

119

View full text Add to dashboard Cite

“…-18 O C -Ter labelling (Rose et al, 1991;A Shevchenko et al, 1997;Uttenweiler-Joseph, Neubauer, Christoforidis, Zerial, & Wilm, 2001), which produces an easily identifiable pattern for the C -Ter peptides (see r section 5.2.6), -Positively (Schwartz & Jardine, 1996;Sonsmann, Romer, & Schomburg, 2002;Yates, Eng, McCormack, & Schieltz, 1995) or negatively (Keough, Lacey, Fieno et al, 2000;Lindh, Hjelmqvist, Bergman, Sjövall, & Griffiths, 2000) charged peptide derivatisation (see section 5.2.5),…”

Section: Figure 14 Esi-ms Spectrum Of Myoglobin (A) and The Reconstrmentioning

confidence: 99%

Acceleration and Improvement of Protein Identification by Mass Spectrometry

Bienvenut¹

2005

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“…188 The fixed-charge derivatization of peptides has also been reported for low-energy CID using an ESI-ion trap mass spectrometer. The introduction of a trimethoxyphenyl phosphonium moiety to the N-terminus of a peptide generates both b-type series ions as well as lessintense a-type ions.…”

Section: ·4 Proteomicsmentioning

confidence: 99%

Biomedical and Biological Mass Spectrometry

Mano

Goto

2003

ANAL. SCI.

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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...

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De novo sequencing of proteolytic peptides by a combination of C-terminal derivatization and nano-electrospray/ collision-induced dissociation mass spectrometry

Cited by 28 publications

References 42 publications

Applications and mechanisms of charge-remote fragmentation

Applications and mechanisms of charge-remote fragmentation

Acceleration and Improvement of Protein Identification by Mass Spectrometry

Biomedical and Biological Mass Spectrometry

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