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Related Concept Videos

Proteomics01:33

Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
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Peptide Identification Using Tandem Mass Spectrometry01:33

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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Updated: Nov 16, 2025

Enhanced Sample Multiplexing of Tissues Using Combined Precursor Isotopic Labeling and Isobaric Tagging cPILOT
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Improved Proteomics-Based Drug Mechanism-of-Action Studies Using 16-Plex Isobaric Mass Tags.

Nico Zinn1, Thilo Werner1, Carola Doce1

  • 1Cellzome GmbH, a GSK Company, Meyerhofstr. 1, 69117 Heidelberg, Germany.

Journal of Proteome Research
|February 23, 2021
PubMed
Summary
This summary is machine-generated.

New 16-plex isobaric mass tags enhance multiplexed quantitative proteomics for sensitive drug target identification. This advancement improves thermal proteome profiling (TPP) and multiplexed proteome dynamics profiling (mPDP) experiments for studying drug interactions.

Keywords:
TMTprothermal proteome profilingtime and condition-based proteome dynamics profiling

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Area of Science:

  • Proteomics
  • Chemical Biology
  • Drug Discovery

Background:

  • Multiplexed quantitative proteomics techniques like thermal proteome profiling (TPP) and multiplexed proteome dynamics profiling (mPDP) are crucial for understanding drug-proteome interactions.
  • Previous isobaric mass tags limited the efficiency and sensitivity of these complex experiments.

Purpose of the Study:

  • To evaluate a new generation of 16-plex isobaric mass tags for enhanced multiplexed quantitative proteomics.
  • To demonstrate sensitive and time-efficient identification of drug targets and proteome-wide effects.

Main Methods:

  • Utilized 16-plex isobaric mass tags for multiplexed quantitative proteomics.
  • Performed thermal proteome profiling (TPP) and 2D-TPP experiments to assess drug-induced changes in protein thermal stability.
  • Employed dynamic SILAC (Stable Isotope Labeling by Amino acids in Cell culture) labeling for proteome-wide analysis of synthesis and degradation rates.

Main Results:

  • Achieved sensitive and time-efficient identification of Staurosporine targets in HepG2 cell extracts using full thermal denaturation profiles in a single mass spectrometry experiment.
  • Comprehensive selectivity profiling of Staurosporine using 2D-TPP demonstrated EC50 values for kinase targets that closely matched the kinobeads gold standard assay.
  • Delineated proteome-wide effects of Indisulam on protein synthesis and degradation rates through multiplexed dynamic SILAC labeling.

Conclusions:

  • The evaluated 16-plex isobaric mass tags significantly improve the efficiency and sensitivity of multiplexed quantitative proteomics workflows.
  • These advanced mass tags enable robust drug target identification and detailed analysis of drug-induced proteome dynamics.
  • The methodology facilitates a deeper understanding of small molecule mechanisms of action and drug response.