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Updated: May 8, 2026
06:17
Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay
Published on: February 28, 2025
New trends in LC protein ligand screening
Marcela C de Moraes1, Kenia L Vanzolini, Carmen L Cardoso
1Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil; Núcleo de Pesquisas de Produtos Naturais, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
Journal of Pharmaceutical and Biomedical Analysis
|August 20, 2013
Summary
Innovative drug discovery requires effective protein ligand screening. This review highlights bioaffinity-based strategies, including chromatography and nanomagnetic methods, for identifying and characterizing protein interactions.
Area of Science:
- Biochemistry
- Drug Discovery
- Analytical Chemistry
Background:
- The discovery of novel therapeutics is driven by the vast array of small molecules and identified biological targets.
- Effective protein ligand screening is crucial for leveraging this diversity to develop innovative drugs.
Purpose of the Study:
- To review recently developed bioaffinity-based strategies for protein ligand screening.
- To critically evaluate chromatographic techniques and their integration with ligand fishing methods.
- To discuss applications in determining protein function, affinity, and activity.
Main Methods:
- Review of bioaffinity-based screening strategies.
- Critical analysis of zonal, frontal, and nonlinear chromatography with immobilized proteins.
- Integration of chromatographic methods with nanomagnetic particle-based ligand fishing.
Main Results:
- Discussion of the utility of various chromatographic elution modes in protein ligand screening.
- Exploration of the synergy between chromatography and nanomagnetic ligand fishing.
- Presentation of applications for characterizing protein parameters.
Conclusions:
- Bioaffinity-based strategies, particularly chromatography coupled with ligand fishing, offer powerful tools for drug discovery.
- These methods enable comprehensive determination of protein function, affinity, and activity.
- Advancements in screening technologies are vital for identifying novel therapeutic agents.
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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...
02:18The Equilibrium Binding Constant and Binding Strength
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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02:04Protein-protein Interfaces
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