Application of mass spectrometry for target identification and characterization

  title={Application of mass spectrometry for target identification and characterization},
  author={Joseph A. Loo and Dana Dejohn and Ping Du and Tracy I. Stevenson and Rachel R. Ogorzalek Loo},
  journal={Medicinal Research Reviews},
Mass spectrometry‐based methodologies span the vast expanse of drug discovery. Both electrospray ionization (ESI) and matrix‐assisted laser desorption/ionization (MALDI) support proteomics‐based research projects by identifying proteins separated and isolated by polyacrylamide gel electrophoresis. MALDI‐MS‐based surface scanning of one‐dimensional isoelectric focusing gels, “virtual 2‐D gel electrophoresis,” represents a potentially high throughput means to map proteins and to determine protein… 

Emerging role of mass spectrometry in structural and functional proteomics.

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  • F. Ahmed
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    Expert review of proteomics
  • 2008
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Electrospray ionisation mass spectrometry (ESI-MS) has been used for the determination and quantitation of a broad range of 24 antibiotics, from groups including aminoglycosides, beta-lactams,

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The results demonstrate the power of PMF of minimally processed microbial cultures as a sensitive and specific technique for the positive identification and phenotypic characterization of certain microorganisms used in biotechnology and bioremediation.

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Technical considerations such as sample preparation methods, resulting analytes, ionization modes, analyzer resolution, and the information provided by respective techniques are discussed in light of sports drug testing requirements using typical application examples.

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High-resolution mass spectrometry is used to study the effects of HIV protease inhibitors on the human zinc metalloprotease ZMPSTE24, which plays a major role in converting prelamin A to mature lamin A and highlights new approaches for documenting off-target drug binding.

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This chapter will explore the role of mass spectrometry (MS) as a detection method for genotyping applications and will illustrate how MS evolved from an expert-user-technology to a routine

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The ability to study specific RNA noncovalent interactions by micron ESI-MS has the potential to provide a unique method by which to analyze and assign precise molecular masses to RNA-RNA complexes.



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The molecular weight measurement of intact Escherichia coli proteins separated by isoelectric focusing‐immobilized pH gradient (IEF‐IPG) gels and analyzed by mass spectrometry is presented. Two

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In many examples of protein complexes, the gas phase‐based measurement is consistent with the expected solution phase binding characteristics, which suggests the utility of ESI‐MS for investigating solution phase molecular interactions.

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Matrix‐assisted laser desorption ionization (MALDI) mass spectra have been obtained directly from thin‐layer isoelectric focusing (IEF) gels with as little as 700 femtomoles of α‐ and β‐chain bovine

Studying noncovalent protein complexes by electrospray ionization mass spectrometry.

  • J. Loo
  • Chemistry, Biology
    Mass spectrometry reviews
  • 1997
Several applications of ESI-MS are discussed, including protein interactions with metal ions and nucleic acids and subunit protein structures (quaternary structure) and mass spectrometry offers advantages in speed and sensitivity.

Mass spectrometry of proteins directly from polyacrylamide gels.

The direct combination of thin-layer gel electrophoresis and matrix-assisted laser desorption/ionization mass spectrometry has been demonstrated with good sensitivity and mass accuracy, offering

Using Electrospray Ionization FTICR Mass Spectrometry To Study Competitive Binding of Inhibitors to Carbonic Anhydrase

The work demonstrates that ESI-MS has significant potential for measuring relative binding affinities and characterizing the structures of ligands associated noncovalently to proteins and should be widely useful in medicinal chemistry.

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This study establishes that mass spectrometry provides the required throughput, the certainty of identification, and the general applicability to serve as the method of choice to connect genome and proteome.

Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels.

Silver staining allows a substantial shortening of sample preparation time and may, therefore, be preferable over Coomassie staining, and this work removes a major obstacle to the low-level sequence analysis of proteins separated on polyacrylamide gels.