Affinity purification of proteins binding to kinase inhibitors immobilized on self-assembling monolayers

Marcus Bantscheff, Scott Hobson, Bernhard Kuster

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

Kinase inhibitors represent a relatively new class of drugs that offer novel therapies targeting specific-malfunctioning kinase-mediated signaling pathways in oncology and potentially inflammation. As the ATP binding sites of the â̂500 human kinases are structurally conserved and because most current drugs target the ATP binding site, there is a need to profile all the kinases that a drug may bind and/or inhibit. We have developed a chemical proteomics method that affinity purifies kinases from cell or tissue lysates using kinase inhibitors immobilized on self-assembling monolayers. The method can be applied to assess the selectivity of a given kinase inhibitor and thus to guide its preclinical or clinical development.

Original languageEnglish
Title of host publicationKinase Inhibitors
Subtitle of host publicationMethods and Protocols
EditorsBernhard Kuster
Pages149-160
Number of pages12
DOIs
StatePublished - 2012

Publication series

NameMethods in Molecular Biology
Volume795
ISSN (Print)1064-3745

Keywords

  • Chemical proteomics
  • Kinase inhibitor
  • Mass spectrometry
  • Self-assembling monolayers

Fingerprint

Dive into the research topics of 'Affinity purification of proteins binding to kinase inhibitors immobilized on self-assembling monolayers'. Together they form a unique fingerprint.

Cite this