Serum Peptide Profiling by Magnetic Particle-Assisted, Automated Sample Processing and MALDI-TOF Mass Spectrometry

Villanueva, Josep; Philip, John; Entenberg, David; Chaparro, Carlos A.; Tanwar, Meena K.; Holland, Eric C.; Tempst, Paul

doi:10.1021/ac0352171

Cited by 438 publications

(374 citation statements)

References 25 publications

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“…Various types of beads have been used, which include reverse-phase chromatographic beads [17,18] and immobilized metal ion beads [19 -21]. To speed up the collection of analyteadsorbed beads from sample solution, magnetic particles, which can be simply collected using a magnet, were developed [22][23][24]. After collection, the microbeads were washed and placed on sample target, followed by analyzing with MALDI MS.…”

mentioning

confidence: 99%

Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS

Chang

Zheng

Chen

et al. 2007

J. Am. Soc. Mass Spectrom.

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Iron oxide nanoparticles modified with oleate have been employed for the extraction of peptides and proteins from aqueous solution before matrix-assisted laser desorption/ionization (MALDI) mass spectrometric (MS) analysis. Adsorption of peptides and proteins onto the nanoparticles were mainly through electrostatic attraction and hydrophobic interaction. The analyte-adsorbed iron oxide nanoparticles could be efficiently collected from solution using a magnet. No elution step was needed. With this preconcentration strategy, the lowest detectable concentration of angiotensin I, insulin, and myoglobin in 500 L of aqueous solution were 0.1 nM, 0.1 nM, and 10.0 nM, respectively. In addition, the nanoparticles could extract the analytes from solution with a high content of salt and surfactant, thus eliminating suppression effect during MALDI MS analysis. This method was successfully applied to concentrate the tryptic digest products of cytochrome c. In addition, the tryptic digestion of cytochrome c can be directly conducted on the iron oxide nanoparticles. atrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) has become a routine analytical tool to determine the molecular mass of biomolecules [1][2][3]. However, samples containing excessive amounts of salts, surfactants, or other contaminations suffer from ionization suppression and adduct formation [4,5]. This limits the application of MALDI technique. Therefore, a simple and selective procedure for extraction and concentration of analyte from complex samples before MALDI MS is required.Various methods have been developed to isolate the analyte from complex sample matrix. In surface-enhanced laser desorption/ionization (SELDI), the sample target played an active role in the extraction, purification, or concentration of the analyte of interest [6 -9]. The target surface was derivatized for the selective retention of analyte while removing interferences through on-target washing. Several surface derivatizations have been designed to extract and concentrate the analyte through hydrophobic interaction [10,11], ionic interaction [12,13], or immunoaffinity [14,15]. However, the sensitivity improvement was limited by the number of binding sites on the target. In another approach, the so-called surface-enhanced affinity capture (SEAC), micrometer-sized beads made for chromatography column were used to capture peptides and proteins from sample solution [16]. Various types of beads have been used, which include reverse-phase chromatographic beads [17,18] and immobilized metal ion beads [19 -21]. To speed up the collection of analyteadsorbed beads from sample solution, magnetic particles, which can be simply collected using a magnet, were developed [22][23][24]. After collection, the microbeads were washed and placed on sample target, followed by analyzing with MALDI MS. Unfortunately, the presence of those particles on the sample target was reported to cause decrease in mass accuracy and resolution [25,26].Recently, nanoparticles have become interesting p...

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mentioning

confidence: 99%

Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS

Chang

Zheng

Chen

et al. 2007

J. Am. Soc. Mass Spectrom.

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“…Novel technology was described by Villanueva et al. (2004) where MALD‐TOF MS was used to simultaneously analyze serum proteins; 1691 peptide masses were identified over the whole dataset. Refinement using a Wilcoxon–Mann U ‐test enabled 274 peptide masses to be identified, differentiating GBM patients and controls, correctly classifying 96.4% of predicted samples as cancerous or not.…”

Section: Mass Spectrometrymentioning

confidence: 99%

A review of novel analytical diagnostics for liquid biopsies: spectroscopic and spectrometric serum profiling of primary and secondary brain tumors

Spalding

Board²,

Dawson

et al. 2016

Brain and Behavior

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IntroductionSpectroscopic and spectrometric analysis of biological samples is regarded as quick, cost effective, easy to operate, and spectroscopic sample preparation involves minimal sample preparation.ResultsTechniques like infrared (IR) spectroscopy, surface‐enhanced laser desorption/ionization (SELDI)‐mass spectroscopy (MS), and matrix‐assisted laser desorption/ionization (MALDI) ‐MS could enable early diagnosis of cancer, disease monitoring, and assessment of treatment responses allowing refinement, if required.DiscussionCarrying out analytical testing within outpatient clinics would dramatically cut the time spent by patients attending different appointments, at different locations, save hospital time and resources but importantly would theoretically enable a reduction in mortality and morbidity. While the advantages of such a prospect seem obvious, this review aims to evaluate the use of human serum spectroscopic and spectrometric analysis as a diagnostic tool for brain cancers, creating a platform for the future of cancer diagnostics.

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“…14 The preparative and analytic processes can be sped up considerably with automation. 29,33 What can we exactly obtain with this method? A spectrum profile that shows hundreds of bars.…”

Section: The Proteome Of the Human Serum And Its Examinationmentioning

confidence: 99%

A path or a new road in laboratory diagnostics? Biological mass spectrometry: Facts and perspectives

Elek

Lapis

2006

Pathol. Oncol. Res.

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Serum Peptide Profiling by Magnetic Particle-Assisted, Automated Sample Processing and MALDI-TOF Mass Spectrometry

Cited by 438 publications

References 25 publications

Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS

Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS

A review of novel analytical diagnostics for liquid biopsies: spectroscopic and spectrometric serum profiling of primary and secondary brain tumors

A path or a new road in laboratory diagnostics? Biological mass spectrometry: Facts and perspectives

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