Advancing Matrix-Assisted Laser Desorption/Ionization-Mass Spectrometric Imaging for Capillary Electrophoresis Analysis of Peptides

Wang, Junhua; Ye, Hui; Zhang, Zichuan; Xiang, Feng; Girdaukas, Gary

doi:10.1021/ac200708f

Cited by 25 publications

(26 citation statements)

References 38 publications

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“…Wang et al. have widely applied CE coupled to MALDI for neuropeptide identification in tissue extracts . Furthermore, CE coupled to MALDI has been also utilized as an analytical tool for the detection of metabolic compounds in complex samples .…”

Section: Coupling Ce To Msmentioning

confidence: 99%

Clinical applications of capillary electrophoresis coupled to mass spectrometry in biomarker discovery: Focus on bladder cancer

Latosinska

Frantzi

Vlahou

et al. 2013

Proteomics Clinical Apps

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A major requirement in the application of proteins as clinical biomarkers is that they provide a highly sensitive and specific result in disease assessment. Since single biomarkers are generally of limited accuracy, a group or panel of well characterized biomarkers appears appropriate, providing a more robust and sensitive mass-spectrometry-based analytical platform. Capillary electrophoresis coupled to MS has been successfully used in biomarker discovery and application, as it enables the selective detection of peptides and small proteins, combining the high separation capacity of CE with the advanced sensitivity of MS. CE-MS allows the characterization of highly complex samples (such as urine, plasma and other biofluids) in a consistent and reproducible way. It has a range of applications, many focusing especially in studies on urinary peptide biomarkers in kidney and cardiovascular diseases. Another major field of interest has been malignancy of the genitourinary system. In the first part of this review we cover technical aspects and performance characteristics of CE-MS, with special focus on the requirements for biomarker discovery and clinical application. In the second part, we review the potential and development of CE-MS in the management of genitourinary cancers, especially bladder cancer (BCa). CE-MS has been employed in several studies aimed at discovering biomarkers for BCa that may be useful in diagnosis, monitoring for recurrence, and prediction of the risk for the muscle-invasive stage. In the last part of the review we discuss current challenges and provide an outlook for ongoing and possible future developments.

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Section: Coupling Ce To Msmentioning

confidence: 99%

Clinical applications of capillary electrophoresis coupled to mass spectrometry in biomarker discovery: Focus on bladder cancer

Latosinska

Frantzi

Vlahou

et al. 2013

Proteomics Clinical Apps

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“…However, the nature of the BGE (presence of salts, volatility) can affect the stability of the spray and then limit the number of BGE that does not prevent the performances of MS. MALDI‐TOF‐MS is an MS technology that presents a greater tolerance to the presence of salts or surfactants . Moreover, hyphenation of electrophoretic methods with MALDI‐MS allows to easily detect positive and negative modes in MS. Then, as an interesting alternative to CE/ESI‐MS, a great number of CE/MALDI‐MS interfaces have been developed . The first strategy to hyphenate electrophoretic method with MALDI‐MS consists of developing online interface .…”

Section: Introductionmentioning

confidence: 99%

Analysis of monoclonal antibody by a novel CE‐UV/MALDI‐MS interface

et al. 2014

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mAbs are highly complex proteins that present a wide range of microheterogeneity that requires multiple analytical methods for full structure assessment and quality control. As a consequence, the characterization of mAbs on different levels is particularly product- and time-consuming. CE-MS couplings, especially to MALDI, appear really attractive methods for the characterization of biological samples. In this work, we report the last instrumental development and performance of the first totally automated off-line CE-UV/MALDI-MS/MS. This interface is based on the removal of the original UV cell of the CE apparatus, modification of the spotting device geometry, and creation of an integrated delivery matrix system. The performance of the method was evaluated with separation of five intact proteins and a tryptic digest mixture of nine proteins. Intact protein application shows the acquisition of electropherograms with high resolution and high repeatability. In the peptide mapping approach, a total number of 154 unique identified peptides were characterized using MS/MS spectra corresponding to average sequence coverage of 64.1%. Comparison with NanoLC/MALDI-MS/MS showed complementarity at the peptide level with an increase of 42% when using CE/MALDI-MS coupling. Finally, this work represents the first analysis of intact mAb charge variants by CZE using an MS detection. Moreover, using a peptide mapping approach CE-UV/MALDI-MS/MS fragmentation allowed 100% sequence coverage of the light chain and 92% of the heavy chain, and the separation of four major glycosylated peptides and their structural characterization.

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“…The benefit of MALDI, soft ionization, and generation of preferentially single charged molecular ions of even large polypeptide and protein macromolecules with M r up 300 000, is employed for the exact determination of M r with an accuracy of ±0.1% and for identification of peptides and proteins isolated by micropreparative CZE (see Section ). A new robust off‐line interface for CE‐MALDI‐MS involves sliding of the capillary outlet end within a machined grove in a MALDI sample plate precoated with a thin layer of matrix for continuous sample deposition . MALDI‐MS imaging by TOF/TOF along the CE track allows high‐resolution and high‐sensitivity detection of peptides, enabling the reconstruction of a CE electropherogram as well as accurate mass measurement and structural identification of peptides.…”

Section: Detectionmentioning

confidence: 99%

Recent developments in capillary and microchip electroseparations of peptides (2011–2013)

Kašička

2013

Electrophoresis

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The review presents a comprehensive survey of recent developments and applications of capillary and microchip electroseparation methods (zone electrophoresis, ITP, IEF, affinity electrophoresis, EKC, and electrochromatography) for analysis, isolation, purification, and physicochemical and biochemical characterization of peptides. Advances in the investigation of electromigration properties of peptides, in the methodology of their analysis, including sample preseparation, preconcentration and derivatization, adsorption suppression and EOF control, as well as in detection of peptides, are presented. New developments in particular CE and CEC modes are reported and several types of their applications to peptide analysis are described: conventional qualitative and quantitative analysis, determination in complex (bio)matrices, monitoring of chemical and enzymatical reactions and physical changes, amino acid, sequence and chiral analysis, and peptide mapping of proteins. Some micropreparative peptide separations are shown and capabilities of CE and CEC techniques to provide relevant physicochemical characteristics of peptides are demonstrated.

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Advancing Matrix-Assisted Laser Desorption/Ionization-Mass Spectrometric Imaging for Capillary Electrophoresis Analysis of Peptides

Cited by 25 publications

References 38 publications

Clinical applications of capillary electrophoresis coupled to mass spectrometry in biomarker discovery: Focus on bladder cancer

Clinical applications of capillary electrophoresis coupled to mass spectrometry in biomarker discovery: Focus on bladder cancer

Analysis of monoclonal antibody by a novel CE‐UV/MALDI‐MS interface

Recent developments in capillary and microchip electroseparations of peptides (2011–2013)

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