Pillar array columns for peptide separations in nanoscale reversed-phase chromatography

Tóth, Gábor; Panić-Janković, Tanja; Mitulović, Goran

doi:10.1016/j.chroma.2019.06.067

Cited by 32 publications

(18 citation statements)

References 34 publications

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“…As the sensitivity of mass spectrometers has greatly improved over the years as a result of e. g. more efficient ionization 19 , ion transfer and detection [20][21][22][23] , further advances in untargeted (also referred to as discovery-type) and data dependent (DDA) proteome analysis may be sought by improving peptide separations [24][25][26] . For example, Gonzalez et al 27 employed a standard 2.1 mm ID analytical column to identify about 800 proteins and 4,000 peptides from 40 µg E. coli protein digest using a 120 min LC gradient.…”

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confidence: 99%

Robust, reproducible and quantitative analysis of thousands of proteomes by micro-flow LC–MS/MS

et al. 2020

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Nano-flow liquid chromatography tandem mass spectrometry (nano-flow LC-MS/MS) is the mainstay in proteome research because of its excellent sensitivity but often comes at the expense of robustness. Here we show that micro-flow LC-MS/MS using a 1 × 150 mm column shows excellent reproducibility of chromatographic retention time (<0.3% coefficient of variation, CV) and protein quantification (<7.5% CV) using data from >2000 samples of human cell lines, tissues and body fluids. Deep proteome analysis identifies >9000 proteins and >120,000 peptides in 16 h and sample multiplexing using tandem mass tags increases throughput to 11 proteomes in 16 h. The system identifies >30,000 phosphopeptides in 12 h and protein-protein or protein-drug interaction experiments can be analyzed in 20 min per sample. We show that the same column can be used to analyze >7500 samples without apparent loss of performance. This study demonstrates that micro-flow LC-MS/MS is suitable for a broad range of proteomic applications.

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confidence: 99%

Robust, reproducible and quantitative analysis of thousands of proteomes by micro-flow LC–MS/MS

et al. 2020

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“…However, the NP stationary phases usually show large heterogeneity, which was also observed in this experiment as a consequence of peak tailing and non-linear retention factors with varying analyte concentrations [80]. Different solvents were used to accomplish elution in NPC, from non-polar organic to some variants like the use of isohydric solvents [81,82]. Some obstacles like lack of retention of highly hydrophilic compounds with ionizable functional groups have been exceeded by ion-exchange chromatography [83] or ion pairing on reversed-phase (RP) columns [84].…”

Section: Clinical Applications 21 Analysis Of Antibioticsmentioning

confidence: 63%

Mass Spectrometry in Clinical Laboratories

Vukajlović¹,

Panić-Janković²

2021

Mass Spectrometry in Life Sciences and Clinical Laboratory

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The analyses performed in clinical laboratories require a high level of precision, selectivity, and sensitivity. The rising number of therapeutic agents from both the field of small and large molecules and the increasing use of modern screening approaches have brought mass spectrometry into almost every clinical laboratory. The need to screen the patients and to follow the therapy’s success can often be fulfilled only by the highly selective and sensitive targeted approach with mass spectrometry. With improving instrument design and miniaturization of the separation technologies, mass spectrometry is no longer an exotic analytical approach. The use of mass spectrometry is now not restricted to the use in a clinical laboratory, but it is used in operating rooms for instant and on-site helping the surgeons with defining the margin of the tissue to be extracted. In this manuscript, we describe the use of mass spectrometry for selected clinical applications and show the possible way of future applications.

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“…Also, Wang et al reported a segmented microfluidic method to pack ultralong up to 5 m capillary columns 104 . In contrast to the packed-bed capillary columns, a micro-pillar array column (μPAC) has recently been demonstrated to be more efficient than particle-packed columns, achieving up to one million theoretical plates at specific conditions 105 . The μPAC leads to much lower back pressure, contributes to higher peak capacity, and identifies a greater number of peptides and proteins from complex samples.…”

Section: Nanotechnology and Nanofabrication Facilitate Lc-ms/ms Analysismentioning

confidence: 99%

Application of nanomaterials in proteomics-driven precision medicine

Zhang

Yang

et al. 2022

Theranostics

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Nanostructured devices and nanoparticles have fundamentally reshaped the development of precision healthcare in recent decades. Meanwhile, mass spectrometry (MS)-based proteomics has evolved from simple protein sequencing to a powerful approach that identifies disease patterns and signatures, reveals molecular mechanisms of pathological processes, and develops therapeutic or preventive drugs. Significantly, the two distinct disciplines have synergized and expanded our knowledge about human health and disease, as evidenced by a variety of nanotechnology-assisted sample processing strategies, facilitating in-depth proteome profiling and post-translational modifications (PTMs) characterization. This review summarizes recent advances in nanoparticle design for better enrichment of marker proteins and their PTMs from various bio-specimens and emerging nanotechnologies that are applied to MS-based proteomics for precision medicine discovery.

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Pillar array columns for peptide separations in nanoscale reversed-phase chromatography

Cited by 32 publications

References 34 publications

Robust, reproducible and quantitative analysis of thousands of proteomes by micro-flow LC–MS/MS

Robust, reproducible and quantitative analysis of thousands of proteomes by micro-flow LC–MS/MS

Mass Spectrometry in Clinical Laboratories

Application of nanomaterials in proteomics-driven precision medicine

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