Mass Spectrometry, Review of the Basics: Electrospray, MALDI, and Commonly Used Mass Analyzers

El‐Aneed, Anas; Cohen, Alejandro; Banoub, Joseph

doi:10.1080/05704920902717872

Cited by 280 publications

(266 citation statements)

References 71 publications

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“…In the context of this discussion certain operational parameters of the ES are discussed for clarity. A more detailed discussion about the ES operational conditions is further provided in section 2.6 and a detailed descriptions of the mechanism of how ES droplets evaporate and charge is transferred to the analyte are provided elsewhere [23,26].…”

Section: Sample Vialmentioning

confidence: 99%

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Electrospray–differential mobility analysis of bionanoparticles

Guha

Tarlov

et al. 2012

Trends in Biotechnology

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The growth of the multibillion dollar bionanoparticle industry has spurred the development of new physical characterization methods. One such method, electrospraydifferential mobility analysis (ES-DMA) constitutes an electrospray for aerosolization of bionanoparticles (such as viruses, gold-nanoparticles, proteins, nanoparticle-protein complexes) and an ion mobility method that operates at atmospheric conditions, and separates bionanoparticles spatially. This dissertation identifies some relevant "problem" areas for ES-DMA by reviewing selected applications.Some such problems are: proteins while passing through ES capillaries are found to interact with it and thus produce time dependent size distributions. Further, it is thought that adsorbed proteins may subsequently desorb and influence size distributions with the ES-DMA which may concomitantly affect quantification of aggregates. These artifacts are studied systematically and it is demonstrated that ES-DMA can quantify adsorption-desorption of complex protein mixtures at high shear rates. Further, it is shown that desorbing proteins do not have a significant effect on size distributions. Another artifact of the ES takes place during the aersolization process. Two units (called monomers) of a bionanoparticle may get encapsulated in the same ES droplet and upon drying of the droplet create artificial dimers thus affecting quantification with ES-DMA. Assuming Poisson distribution, this thesis provides a systematic approach that can be undertaken to eliminate this artifact. A third artifact arises from the low sensitivity of the DMA to size increase. When a ligand (for e.g. protein) adsorbs to a bionanoparticle it creates an increase in the size of the later, which can be used to quantify the amount of ligand adsorbed per bionanoparticle. As ligands can change conformations upon adsorption, using ES-DMA for such applications may be flawed. This issue has been identified and a solution has been provided by integrating a mass analyzer after the ES-DMA.After correcting for these artifacts, this dissertation delves into characterization of different types of bionanoparticles and demonstrates that ES-DMA has several advantages over other traditional techniques such as transmission electron microscopy, size exclusion chromatography, analytical ultracentrifugation, dynamic light scattering and plaque assay and thus has immense potential to become a process analytical technique in biomanufacturing environments. ELECTROSPRAY-DIFFERENTIAL MOBILITY ANALYSIS OF BIONANOPARTICLES

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Section: Sample Vialmentioning

confidence: 99%

“…The neutralizer is the second component of the ES-DMA and is the primary way of charging the analytes in ES-DMA unlike mass spectrometry (MS) [23,26].…”

Section: Neutralization Chambermentioning

confidence: 99%

Electrospray–differential mobility analysis of bionanoparticles

Guha

Tarlov

et al. 2012

Trends in Biotechnology

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“…Several reviews have been published recently, describing in detail this technique and its application in proteomics (11)(12)(13)(14)(15). Herein, the general concepts necessary for understanding the use of mass spectrometry for detecting PTMs will be briefly reviewed.…”

Section: Mass Spectrometrymentioning

confidence: 99%

“…Several ionization methods have been developed for analyzing organic compounds (13,16). However, the development of two soft ionization techniques capable of ionizing non-volatile and thermo-unstable biological compounds, namely electrospray ionization (ESI) (17) and matrix-assisted laser desorption/ionization (MALDI) (18,19), allowed protein analysis using MS. For a detailed view of the ionization mechanisms, the interested reader is referred to specialist reviews for ESI (20) and MALDI (21).…”

Section: Mass Spectrometrymentioning

confidence: 99%

Post-translational Modifications and Mass Spectrometry Detection

Silva

Vitorino

Domingues

et al. 2013

Free Radical Biology and Medicine

105

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In this review, we provide a comprehensive bibliographic overview of the role of mass spectrometry and the recent technical developments in the detection of post-translational modifications (PTMs). We briefly describe the principles of mass spectrometry for detecting PTMs and the protein and peptide enrichment strategies for PTM analysis, including phosphorylation, acetylation and oxidation. This review presents a bibliographic overview of the scientific achievements and the recent technical development in the detection of PTMs is provided. In order to ascertain the state of the art in mass spectrometry and proteomics methodologies for the study of PTMs, we analyzed all the PTM data introduced in the Universal Protein Resource (UniProt) and the literature published in the last three years. The evolution of curated data in UniProt for proteins annotated as being posttranslationally modified is also analyzed. Additionally, we have undertaken a careful analysis of the research articles published in the years 2010 to 2012 reporting the detection of PTMs in biological samples by mass spectrometry.

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“…Unlike high performance liquid chromatography (HPLC), MALDI-TOF mass spectrometry allows the direct analysis of large intact bioactives without the need for analyte separation prior to analysis [4]. However, peptide quantification with MALDI-TOF mass spectrometry can be difficult due to the signal-to-signal suppression and the unreliability of using analyte signal to noise ratio for quantification purposes.…”

Section: Introductionmentioning

confidence: 99%

Quantification of Cell-Penetrating Peptide Associated with Polymeric Nanoparticles Using Isobaric-Tagging and MALDI-TOF MS/MS

Chiu

Tucker

McDowell

2016

J. Am. Soc. Mass Spectrom.

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Abstract. High sensitivity quantification of the putative cell-penetrating peptide diarginine-histidine (RRH) associated with poly (ethyl-cyanoacrylate) (PECA) nanoparticles was achieved without analyte separation, using a novel application of isobarictagging and high matrix-assisted laser desorption/ionization coupled to time-of-flight (MALDI-TOF) mass spectrometry. Isobaric-tagging reaction equilibrium was reached after 5 min, with 90% or greater RRH peptide successfully isobaric-tagged after 60 min. The accuracy was greater than 90%, which indicates good reliability of using isobarictagged RRH as an internal standard for RRH quantification. The sample intra-and inter-spot coefficients of variations were less than 11%, which indicate good repeatability. The majority of RRH peptides in the nanoparticle formulation were physically associated with the nanoparticles (46.6%), whereas only a small fraction remained unassociated (13.7%). The unrecovered RRH peptide (~40%) was assumed to be covalently associated with PECA nanoparticles.

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Mass Spectrometry, Review of the Basics: Electrospray, MALDI, and Commonly Used Mass Analyzers

Cited by 280 publications

References 71 publications

Electrospray–differential mobility analysis of bionanoparticles

Electrospray–differential mobility analysis of bionanoparticles

Post-translational Modifications and Mass Spectrometry Detection

Quantification of Cell-Penetrating Peptide Associated with Polymeric Nanoparticles Using Isobaric-Tagging and MALDI-TOF MS/MS

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