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Related Concept Videos

Proteomics01:33

Proteomics

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 proteomics...

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Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays
13:22

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Published on: October 23, 2019

Kinase inhibitor profiling using chemoproteomics.

Markus Schirle1, Eugene C Petrella, Scott M Brittain

  • 1Novartis Institutes for Biomedical Research, Cambridge, MA, USA. markus.schirle@novartis.com

Methods in Molecular Biology (Clifton, N.J.)
|October 1, 2011
PubMed
Summary

Quantitative chemoproteomics reveals small molecule interactions with endogenous kinases. This method, using dose-dependent competition and mass spectrometry, ranks kinase inhibitor binding affinities under physiological conditions.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Pharmacology

Background:

  • Quantitative chemoproteomics enables profiling of small molecule-protein interactions in cells.
  • Traditional kinase assays lack physiological relevance compared to cellular approaches.

Purpose of the Study:

  • To apply quantitative chemoproteomics for determining kinase inhibitor binding profiles.
  • To rank kinase inhibitor binding affinities under near-physiological conditions.

Main Methods:

  • Utilized a dose-dependent, competition-based experimental design.
  • Employed quantitative mass spectrometry with tandem mass tags (TMT) for isobaric labeling.
  • Assessed compound binding to endogenously expressed kinases.

Main Results:

  • Established a method to determine protein interaction profiles of small molecules.
  • Demonstrated the ability to rank kinase inhibitor interactions by binding affinity.
  • Achieved conditions approximating the physiological state of kinases.

Conclusions:

  • Quantitative chemoproteomics is a powerful approach for kinase inhibitor profiling.
  • This method provides a more physiologically relevant assessment of drug-target interactions.
  • Tandem mass tag (TMT) labeling facilitates accurate affinity ranking.