Related Experiment Video
Updated: May 21, 2025

Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay
Published on: February 28, 2025
Quantitative proteomics and applications in covalent ligand discovery.
Ananya A Basu1,2, Xiaoyu Zhang1,2,3,4,5
1Department of Chemistry, Northwestern University, Evanston, IL 60208.
Multiplexing technologies in proteomics allow for large-scale protein quantification. This review explores quantitative proteomic techniques crucial for covalent ligand discovery, enhancing selectivity profiling and mechanistic understanding.
Area of Science:
- Biochemistry
- Analytical Chemistry
- Pharmacology
Background:
- Proteomics enables large-scale protein quantification with high confidence.
- Quantitative proteomics is vital for understanding lead compound mechanisms in drug discovery.
- High-throughput screening demands efficient analytical methods.
Purpose of the Study:
- To review quantitative proteomic techniques for covalent ligand discovery.
- To highlight the role of these techniques in selectivity profiling.
- To discuss how proteomics can inform mechanistic insights.
Main Methods:
- Discussion of various quantitative proteomic techniques.
- Focus on multiplexing systems capable of analyzing multiple samples.
- Integration of proteomic data with covalent ligand discovery workflows.
Main Results:
- Multiplexing systems can analyze up to 18 samples per run.
- Quantitative proteomics provides critical mechanistic insights.
- Proteomic analyses can match the pace of high-throughput workflows.
Conclusions:
- Quantitative proteomics is essential for advancing covalent ligand discovery.
- Multiplexing technologies significantly enhance the efficiency of proteomic studies.
- These methods offer a powerful approach for establishing compound selectivity profiles.
More Related Videos
10:36Covalent Labeling with Diethylpyrocarbonate for Studying Protein Higher-Order Structure by Mass Spectrometry
Published on: June 15, 2021
10:01Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
Published on: November 28, 2017
Related Concept Videos
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
The Equilibrium Binding Constant and Binding Strength
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Ligand Binding and Linkage
Complexometric Titration: Ligands
Protein-protein Interfaces