Preparative Linear Ion Trap Mass Spectrometer for Separation and Collection of Purified Proteins and Peptides in Arrays Using Ion Soft Landing

Blake, Thomas A.; Ouyang, Zheng; Wiseman, Justin M.; Takáts, Zoltán; Guymon, Andrew J.; Kothari, Sameer; Cooks, R. Graham

doi:10.1021/ac048981b

Cited by 73 publications

(77 citation statements)

References 49 publications

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“…The soft-landing of mass-selected multiply-charged ions was achieved using a single-stage quadrupole model SSQ-710C (Thermo Finnigan, Bremen, Germany) or by using a home-built linear ion trap mass spectrometer (SL1.0) [37]. The SSQ instrument ( Figure 1a) was modified to allow a surface to be positioned in the vacuum chamber.…”

Section: Instrumentationmentioning

confidence: 99%

“…A diagram of the linear trap instrument (LIT) is shown in Figure 1b and its detailed operation is described elsewhere [37]. This instrument includes an ESI ion source, a high-capacity LIT, wave form capabilities for ion isolation, a radial detector for mass analysis, and facilities for low energy transfer of trapped, massselected ions onto specific spots onto an electronically movable target.…”

Section: Instrumentationmentioning

confidence: 99%

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Ion soft-landing into liquids: Protein identification, separation, and purification with retention of biological activity

Gologan

Takáts

Alvarez

et al. 2004

J. Am. Soc. Mass Spectrom.

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122

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Protein ions, after mass spectrometric separation, can be soft-landed into liquid surfaces with preservation of their native structures. Retention of biological activity is strongly favored in glycerol-based surfaces but not in self-assembled monolayer solid surfaces. Soft-landing efficiency for multiply-charged hexokinase ions was found to be some four times higher for a glycerol/fructose liquid surface than for a fluorinated self-assembled monolayer surface. Soft-landing into liquid surfaces is also shown to allow (1) protein purification, (2) on-surface identification of the soft-landed material using MALDI, and (3) protein identification by in-surface tryptic digestion. Pure lysozyme was successfully isolated from different mixtures including an oxidized, partially decomposed batch of the protein and a partial tryptic digest. Liquid glycerol/carbohydrate mixtures could be used directly to record MALDI spectra on the soft-landed compounds provided they were fortified in advance with traditional MALDI matrices such as p-nitroaniline and ␣-cyano-4-hydroxycinnamic acid. Various proteins were soft-landed and detected on-target using these types of liquid surface. Soft-landing of multiply-charged lysozyme ions onto fluorinated self-assembled monolayer surfaces was found to occur with a limited amount of neutralization, and trapped multiply-charged ions could be desorbed from the surface by laser desorption. Initial data is shown for a new approach to protein identification that combines top-down and bottom-up approaches by utilizing protein ion soft-landing from a protein mixture, followed by tryptic digestion of the landed material and detection of characteristic tryptic fragments by MALDI. , has been applied in experiments ranging from studies using chemically inert and structurally organized self-assembled monolayers (SAMs) as substrates for ion storage [2], to studies of ion mobility through ice and vapor deposited films [3,4], to experiments aimed at developing a separation method in a form of preparatory mass spectrometry [5,6]. Simple organic cations [7,8] [12][13][14] have all been the targets of examination by ion soft-landing. The separation, purification, and storage of chemical species by a completely non-destructive, mass spectrometric approach are the objectives of the studies currently underway in our laboratory.In a preliminary report [5], we described a method which showed the potential for generating biologically active protein chips from protein mixtures by massselective ion soft-landing. After ionization of the mixture by electrospray (ESI), individual protein ions were mass-selected and soft-landed at predetermined locations on the surface. The results showed that the use of mass spectrometry as a separation method in biology provides high selectivity because components with different molecular formulas can be separated and softlanded. However, retention of the biological activity of a protein or other biomolecule in the course of this (or any mass spectrometry experiment) is a much more chall...

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Section: Instrumentationmentioning

confidence: 99%

Section: Instrumentationmentioning

confidence: 99%

Ion soft-landing into liquids: Protein identification, separation, and purification with retention of biological activity

Gologan

Takáts

Alvarez

et al. 2004

J. Am. Soc. Mass Spectrom.

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122

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“…Ion traps, especially 2D linear ion traps, have been widely used in hybrid instruments as the trapping devices for reactions in front of the final stage for mass analysis [8 -10]. rf-Driven ion optical components, such as the quadrupole (or "square quad"), are commonly used as ion guides over various pressure ranges [11][12][13]. Under appropriate operating conditions, such devices could potentially be used as linear traps or quadrupole filters to perform mass-selective operations, either alone or in tandem with other mass analyzers.…”

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confidence: 99%

Ion trap mass analysis at high pressure: A theoretical view

Song

Smith

et al. 2009

J. Am. Soc. Mass Spectrom.

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The mass-selective manipulation of ions at elevated pressure, including mass analysis, ion isolation, or excitation, is of great interest for the development of mass spectrometry instrumentation, particularly for systems in which ion traps are employed as mass analyzers or storage devices. While experimental exploration of high-pressure mass analysis is limited by various difficulties, such as ion detection or electrical discharge at high-pressure, theoretical methods have been developed in this work to study ion/neutral collision effects within quadrupole ion traps and to explore their performance at pressures up to 1 Torr. Ion trapping, isolation, excitation, and resonance ejection were investigated over a wide pressure range. The theoretically calculated data were compared with available experimental data for pressures up to 50 mTorr, allowing the prediction of ion trap performance at pressures more than 10 times higher. (J Am Soc Mass

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“…A totally different approach to fabricate peptide arrays was followed by Blake et al [148]. They developed a preparative mass spectrometer for the production of protein arrays using the ion soft landing technique to collect ions on a surface after separation by mass/charge ratio.…”

Section: Immobilization Of Pre-synthesized Peptidesmentioning

confidence: 99%

Microarray Technology as a Universal Tool for High-Throughput Analysis of Biological Systems

Sobek¹,

Bartscherer²,

Jacob³

et al. 2006

CCHTS

110

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Over the last years microarray technology has become one of the principal platform technologies for the highthroughput analysis of biological systems. Starting with the construction of first DNA microarrays in the 1990s, microarray technology has flourished in the last years and many different new formats have been developed. Peptide and protein microarrays are now applied for the elucidation of interaction partners, modification sites and enzyme substrates. Antibody microarrays are envisaged to be of high importance for the high-throughput determination of protein abundances in translational profiling approaches. First cell microarrays have been constructed to transform microarray technology from an in vitro technology to an in vivo functional analysis tool. All of these approaches share a common prerequisite: the solid support on which they are generated. The demands on this solid support are thereby as manifold as the applications themselves. This review is aimed to display the recent developments in surface chemistry and derivatization, and to summarize the latest developments in the different application areas of microarray technology.

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Preparative Linear Ion Trap Mass Spectrometer for Separation and Collection of Purified Proteins and Peptides in Arrays Using Ion Soft Landing

Cited by 73 publications

References 49 publications

Ion soft-landing into liquids: Protein identification, separation, and purification with retention of biological activity

Ion soft-landing into liquids: Protein identification, separation, and purification with retention of biological activity

Ion trap mass analysis at high pressure: A theoretical view

Microarray Technology as a Universal Tool for High-Throughput Analysis of Biological Systems

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