Desorption ionization mass spectrometry: sample preparation for secondary ion mass spectrometry, laser desorption, and field desorption

Busch, Kenneth L.; Unger, Steve; Vincze, A.; Cooks, R. Graham; Keough, T.

doi:10.1021/ja00370a009

Cited by 131 publications

(53 citation statements)

References 3 publications

(3 reference statements)

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“…Some of these derivatives contained nonpolar functionalities to increase the surface activities of peptides during analysis by FAB and LSIMS (Falick & Maltby, 1989;Ligon, 1986;Naylor et al, 1986). Other derivatives generated preformed ions, which increased ionization efficiencies of many analytes during analysis by desorption/ionization techniques (Busch et al, 1982).…”

Section: Introductionmentioning

confidence: 99%

Charge derivatization of peptides for analysis by mass spectrometry

Roth¹,

Huang²,

Sadagopan³

et al. 1998

Mass Spectrom. Rev.

133

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Section: Introductionmentioning

confidence: 99%

Charge derivatization of peptides for analysis by mass spectrometry

Roth¹,

Huang²,

Sadagopan³

et al. 1998

Mass Spectrom. Rev.

133

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“…Positively charged derivatives have been used in desorption mass spectrometry for many years to improve sensitivity by enhancing ionization efficiencies (11,12). Localization of a positive charge at a particular site on a peptide (13,14) also profoundly affects the nature of the fragment ions observed in high-collision energy tandem mass spectrometry (15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26).…”

mentioning

confidence: 99%

A method for high-sensitivity peptide sequencing using postsource decay matrix-assisted laser desorption ionization mass spectrometry

Keough

Youngquist

Lacey

1999

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

225

262

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A method has been developed for de novo peptide sequencing using matrix-assisted laser desorption ionization mass spectrometry. This method will facilitate biological studies that require rapid determination of peptide or protein sequences, e.g., determination of posttranslational modifications, identification of active compounds isolated from combinatorial peptide libraries, and the selective identification of proteins as part of proteome studies. The method involves fast, one-step addition of a sulfonic acid group to the N terminus of tryptic peptides followed by acquisition of postsource decay (PSD) fragment ion spectra. The derivatives are designed to promote efficient charge site-initiated fragmentation of the backbone amide bonds and to selectively enhance the detection of a single fragment ion series that contains the C terminus of the molecule (y-ions). The overall method has been applied to pmol quantities of peptides. The resulting PSD fragment ion spectra often exhibit uninterrupted sequences of 20 or more amino acid residues. However, fragmentation efficiency decreases considerably at amide bonds on the C-terminal side of Pro. The spectra are simple enough that de novo sequence tagging is routine. The technique has been successfully applied to peptide mixtures, to high-mass peptides (up to 3,600 Da) and to the unambiguous identification of proteins isolated from two-dimensional gel electrophoresis. The PSD spectra of these derivatized peptides often allow far more selective protein sequence database searches than those obtained from the spectra of native peptides.Knowledge of protein sequences is fundamentally important for understanding many physiological processes at the molecular level (1). Tandem mass spectrometry has become an increasingly essential tool for protein and peptide sequencing because of its speed, sensitivity, and applicability to complex mixtures (2). Recently, postsource decay (PSD) matrix-assisted laser desorption ionization (MALDI) mass spectrometry was developed for high-sensitivity peptide sequencing applications (3-8). Subpicomole limits of analysis were reported as a result of the high yield of fragment ions and the high ion transmission inherent with time-of-flight mass spectrometry (5). Kaufmann et al. (5) also noted several problems associated with PSD MALDI sequencing of peptides, including the complexity of the resulting fragmentation patterns and the lack of computer algorithms capable of interpreting the complex spectra. The recent incorporation of delayed extraction (DE) (9, 10), a technique designed to improve precursor-ion mass resolution and mass-measurement accuracy, reduced the rate of PSD fragmentation by at least an order of magnitude. As a result, many low-intensity precursor ions obtained by DE MALDI do not produce enough PSD fragmentation to allow derivation of even short sequence tags (7).Positively charged derivatives have been used in desorption mass spectrometry for many years to improve sensitivity by enhancing ionization efficiencies (11, 12...

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“…To increase the secondary ion yield for a number of species separated by TLC, a series of derivation reactions were developed that transfer the same molecules into preformed ions, often with surfactant properties in the matrix that is ultimately used for their extraction. The original concept of ionic derivatization was described by Busch et al (83); methods of sample derivatization that do not increase the size of the samples were developed based on the voluminous TLC derivatization literature. Such derivatizations can be used in TLC/SIMS to increase the secondary ion yield of the separated compounds without an increase in the spot size (84,85).…”

Section: Buschmentioning

confidence: 99%

Thin-Layer Chromatography Coupled with Mass Spectrometry

Busch¹

2003

Handbook of Thin-Layer Chromatography

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Desorption ionization mass spectrometry: sample preparation for secondary ion mass spectrometry, laser desorption, and field desorption

Cited by 131 publications

References 3 publications

Charge derivatization of peptides for analysis by mass spectrometry

Charge derivatization of peptides for analysis by mass spectrometry

A method for high-sensitivity peptide sequencing using postsource decay matrix-assisted laser desorption ionization mass spectrometry

Thin-Layer Chromatography Coupled with Mass Spectrometry

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