Review of a current role of mass spectrometry for proteome research

Chen, Chung-Hsuan Winston

doi:10.1016/j.aca.2008.06.017

Cited by 95 publications

(57 citation statements)

References 120 publications

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“…N-PAGE and BN-PAGE, different from all SDS-PAGE-based electrophoresis, are capable of separating native and catalytic active membrane proteins, which avoid the denaturation of proteins with SDS [13,14]. Currently, 1-D gel is more often used for proteomic analysis [3]. The principle of SDS-PAGE is that electrophoretic mobility of protein is relevant only to its M r since the use of SDS and b-mercaptoethanol (BME) or DTT, which denatures original proteins and eliminates protein's original surface charge and form, then gives rise to M r -based SDS-protein complex [15].…”

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confidence: 99%

Ionic liquid‐assisted SDS‐PAGE to improve human serum protein separation

Zhang

Gai

et al. 2011

Electrophoresis

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Ionic liquid (IL)-assisted sodium dodecyl sulfate polyacrylamide gel electrophoresis (ILs-SDS-PAGE) was presented to improve protein separation. ILs were employed during the preparation process of polyacrylamide gel, then the modified gel was used for commercial protein marker, binary bovine serum albumin/lysozyme (BSA/Lyz) and human serum separation. The influence of ionic liquid concentration, cation alkyl chain length, cation and anion types on proteins separation were investigated. The results showed that ILs played a role in improving some protein separation, and ILs-SDS-PAGE provided higher resolution and separation efficiency than ordinary SDS-PAGE for low and middle relative molecular mass proteins in human serum. In addition, the principle of ILs-SDS-PAGE was discussed and the comparison of ILs-SDS-PAGE with ordinary SDS-PAGE and Native PAGE was made.

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confidence: 99%

Ionic liquid‐assisted SDS‐PAGE to improve human serum protein separation

Zhang

Gai

et al. 2011

Electrophoresis

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“…In the "bottom-up" approach, purified proteins or complex protein mixtures are subjected to chemical or enzymatic cleavage, and the peptide products are usually separated by chromatography followed by the tandem mass spectrometry analysis. In the "top-down" approach, intact protein ions or large protein fragments are directly subjected to the gas-phase fragmentation for MS analysis (47). Given the complexity in protein structures, a single approach may not be sufficient to provide comprehensive information for the structure identification purpose.…”

Section: Structure Elucidation For In Vivo Degradants and Isoforms Ofmentioning

confidence: 99%

“…Two fundamental strategies for MS analysis of protein structures are the "bottom-up" and the "top-down" approaches (46)(47)(48). In the "bottom-up" approach, purified proteins or complex protein mixtures are subjected to chemical or enzymatic cleavage, and the peptide products are usually separated by chromatography followed by the tandem mass spectrometry analysis.…”

Section: Structure Elucidation For In Vivo Degradants and Isoforms Ofmentioning

confidence: 99%

Challenges and Opportunities in Absorption, Distribution, Metabolism, and Excretion Studies of Therapeutic Biologics

Vugmeyster

2012

AAPS J

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Abstract. With the advancement of biotechnology in the last two decades, optimized and novel modalities and platforms of biologic moieties have emerged rapidly in drug discovery pipelines. In addition, new technologies for delivering therapeutic biologics (e.g., needle-free devices, nanoparticle complexes), as well as novel approaches for disease treatments (e.g., stem cell therapy, individualized medicine), continue to be developed. While pharmacokinetic studies are routinely carried out for therapeutic biologics, experiments that elucidate underlying mechanisms for clearance and biodistribution or identify key factors that govern absorption, distribution, metabolism, and excretion (ADME) of biologics often are not thoroughly conducted. Realizing the importance of biologics as therapeutic agents, pharmaceutical industry has recently begun to move the research focus from small molecules only to a blended portfolio consisting of both small molecules and biologics. This trend brings many opportunities for scientists working in the drug disposition research field. In anticipation of these opportunities and associated challenges, this review highlights impact of ADME studies on clinical and commercial success of biologics, with a particular focus on emerging applications and technologies and linkage with mechanistic pharmacokinetic/pharmacodynamic modeling and biomarker research.

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“…Mass spectrometry is also useful when there is no prior knowledge of the proteins and works through the mass analyzers time-of-fl ight, quadrupole, Fourier transform ion cyclotron resonance, ion trap, Fourier transform infrared spectroscopy, coupled plasma, and electrospray ionization, which can be combined in one mass spectrometer with a dynamic range of up to four orders of magnitude. The determination of geometric structures is done using nuclear magnetic resonance or X-ray crystallography, and collision-induced dissociation is used to obtain the fragmentation pattern of the peptides/ protein [Chacón- Lee et al, 2010;Chen, 2008;Bernal et al, 2014].…”

Section: Foodomics and Microalgal Bioactive Compoundsmentioning

confidence: 99%