Online CE−MALDI-TOF MS Using a Rotating Ball Interface

Musyimi, Harrison K.; Narcisse, Damien A.; Zhang, Xia; Stryjewski, Wiesław; Soper, Steven A.; Murray, Kermit K.

doi:10.1021/ac0489723

Cited by 62 publications

(56 citation statements)

References 35 publications

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“…[67][68][69][70][71][72][73][74][75][76][77][78][79][80][81][82][83] Only these two configurations are covered in this review, although, brief descriptions of the other three are given in the succeeding paragraphs.…”

Section: Ionization Methodsmentioning

confidence: 99%

“…76 Ørsnes et al 67 constructed an interface based on a rotating ball inlet (ROBIN), in which the sample adhering to the surface of the ball is continuously carried past a polymer gasket into the vacuum chamber. Musyimi et al 83 modified this design so that the majority of the ball surface is at atmospheric pressure and easily accessible for sample deposition.…”

Section: ·2 Maldi-time-of-flight(tof)-msmentioning

confidence: 99%

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Recent Developments in Capillary Electrophoresis–Mass Spectrometry of Proteins and Peptides

Monton

Terabe

2005

ANAL. SCI.

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Many researchers have invested considerable efforts toward improving capillary electrophoresis (CE)-mass spectrometry (MS) systems so they can be applied better to standard analyses. This review highlights the developments in CE-MS of proteins and peptides over the last five years. It includes the developments in interfaces, sample-enrichment techniques, microfabricated devices, and some applications, largely in capillary zone electrophoresis (CZE), capillary isoelectric focusing (CIEF) and capillary isotachophoresis formats.

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Section: Ionization Methodsmentioning

confidence: 99%

Section: ·2 Maldi-time-of-flight(tof)-msmentioning

confidence: 99%

Recent Developments in Capillary Electrophoresis–Mass Spectrometry of Proteins and Peptides

Monton

Terabe

2005

ANAL. SCI.

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“…In contrast to direct CE-MS coupling using electrospray, coupling of CE to MALDI-MS by deposition of the analytes onto different targets has also been described [37]; for example, a rotating ball interface which allows online coupling of CE to MALDI-MS. The main advantages of MALDI appear to be enhanced stability (in comparison to ESI) and effortless handling.…”

Section: Technical Aspects Of Ce-ms Couplingmentioning

confidence: 99%

“…Consequently, polypeptides of interest must be uniquely defined by highly accurate mass and, if possible, additional identifying parameters (e.g., migration time) in order to be isolated and sequenced using MS/MS. Like HPLC, the CE can either be directly interfaced with an MS/MS instrument or the entire CE run can be spotted onto a MALDI target plate and subsequently the polypeptides of interest can be analyzed [37,47,55]. With the latter approach, the entire CE-MS run is immobilized and the single fractions (spots) can be analyzed repeatedly without the need of a new CE run.…”

Section: Identification Of Polypeptides By Ms/ms Sequencingmentioning

confidence: 99%

Capillary electrophoresis coupled to mass spectrometry for clinical diagnostic purposes

2005

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Capillary electrophoresis coupled to mass spectrometry for clinical diagnostic purposesThe introduction of fast, sensitive, and robust techniques for proteomic analysis into clinical practice represents a major step toward a new diagnostic approach of body fluids. In addition, proteomics emerges as a key technology for the discovery of disease biomarkers in various body fluids. However, even in relatively protein-deprived body fluids such as urine, the complexity and wide dynamic range of protein expression pose a considerable challenge to both separation and identification technologies. In the present review we discuss from a clinical point-of-view recent advances of the use of proteomics in clinical diagnosis as well as therapy evaluation. We focus on capillary electrophoresis coupled to mass spectrometry (CE-MS) and discuss CE-MS from an application point of view evaluating its merits and vices with regard to biomarker discovery. This review further presents examples of clinical applications of CE-MS for detection and identification of biomarkers in urine. IntroductionIt is well appreciated for centuries that body fluids contain information on the "internal" environment, i.e., the function of tissues and organs, which can be used as a gauge for the well being of the organism. Although this concept was created by Hippocrates more than 2000 years ago, standardized clinical laboratory tests were not developed before the 20th century. Moreover, a systematic discovery of biomarkers was made possible only with the discovery of antibodies and their use in immunological assays such as radioimmuno assay (RIA), ELISA, etc. Their increasing use enabled detection and quantification of distinct molecules -mainly peptides and proteins -in various body fluids. However, these techniques were limited by their requirement of prior knowledge of the molecule and a specific probe. New functional proteomic approaches appeared to circumvent these limitations. Spurred by advances in MS it was hoped that proteomics would allow the analysis of thousands of peptides and proteins in one sample [1][2][3][4][5][6], but several obstacles turned up soon. The high complexity and wide dynamic range of peptides in body fluids required pre-MS separation techniques that offer high resolution and could cope with a wide dynamic range of peptide concentrations [3]. Further, suitable software for interpretation of a vast number of generated MS spectra as well as comparison of the data was a major challenge [7].The approach towards solving most of these problems was to reduce data complexity, for example by arbitrarily collecting data on only a few polypeptides and also to reduce resolution of the analysis instrument. Both were accomplished with the surface-enhanced laser desorption/ionization (SELDI) technology -a complex solution of analytes was allowed to interact with an active surface (ion-exchange, hydro-

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“…We have developed a new version of the rotating ball inlet that addresses the design issues of the previous version [23]. The system is constructed so that more than half of the ball interface is exposed to atmospheric pressure and can be used for either direct contact or non-contact sample deposition.…”

mentioning

confidence: 99%