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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...
Immunoprecipitation01:20

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...

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Related Experiment Video

Updated: Jul 4, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

An immuno-chemo-proteomics method for drug target deconvolution.

Chaitanya Saxena1, Eugene Zhen, Richard E Higgs

  • 1Integrative Biology, Greenfield Laboratories, Eli Lilly and Company, Greenfield, IN 46140, USA. saxena_chaitanya@lilly.com

Journal of Proteome Research
|July 2, 2008
PubMed
Summary
This summary is machine-generated.

A novel soluble probe method improves drug target deconvolution by coupling small molecules to peptide epitopes. This chemical proteomics approach verifies compound binding and identifies new drug targets, overcoming limitations of solid-phase methods.

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Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
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Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Area of Science:

  • Chemical proteomics
  • Drug discovery
  • Molecular biology

Background:

  • Chemical proteomics aids drug target deconvolution and toxicity profiling.
  • Small molecules immobilized on solid supports are common but their affinity post-immobilization is hard to assess.

Purpose of the Study:

  • To develop and validate a soluble probe method for chemical proteomics.
  • To overcome limitations of solid-phase immobilization in evaluating compound-target interactions.
  • To identify novel targets of the PKC-alpha inhibitor Bisindolylmaleimide-III.

Main Methods:

  • Developed a soluble probe by coupling Bisindolylmaleimide-III with a FLAG epitope peptide.
  • Used anti-FLAG antibody beads for affinity isolation of bound proteins from cell lysates.
  • Compared the soluble probe method with traditional solid-phase immobilization.

Main Results:

  • The soluble probe confirmed Bisindolylmaleimide-III retained binding characteristics after coupling.
  • Identified known targets (PKC-alpha, GSK3-beta, etc.) and novel targets (PKAC-alpha, prohibitin, VDAC, heme binding proteins).
  • The method provided an orthogonal strategy to the solid-phase approach, aiding target deconvolution and reducing false positives.

Conclusions:

  • The soluble probe method is effective for chemical proteomics and drug target deconvolution.
  • This approach allows direct verification of compound binding affinity.
  • It offers an orthogonal strategy to solid-phase methods, enhancing accuracy in target identification.