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Updated: Aug 8, 2026
13:49
Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates
Published on: December 6, 2017
Protein affinity map of chemical space
L M Kauvar1, H O Villar, J R Sportsman
1Terrapin Technologies, Inc., San Francisco, CA 94080, USA.
Journal of Chromatography. B, Biomedical Sciences and Applications
|October 29, 1998
Summary
Affinity fingerprinting maps chemical space using protein binding preferences. This method efficiently identifies active drug ligands from large compound libraries, aiding drug discovery and target classification.
Area of Science:
- Chemical biology
- Proteomics
- Drug discovery
Background:
- Mapping chemical space is crucial for drug discovery.
- Existing methods for ligand identification can be time-consuming and resource-intensive.
Purpose of the Study:
- To introduce and validate affinity fingerprinting as a quantitative method for mapping chemical space.
- To demonstrate its utility in identifying active ligands for specific protein targets and categorizing therapeutic targets.
Main Methods:
- Utilizing a reference panel of fewer than 20 proteins to capture differential compound-protein interactions.
- Iteratively sampling chemical space based on affinity fingerprints.
- Assaying fewer than 200 compounds against specific protein targets for validation.
Main Results:
- Successfully identified active ligands from a library of 30,000 compounds for diverse protein targets.
- Demonstrated that a small reference panel (<20 proteins) can effectively differentiate compound interactions.
- Developed a strategy for selecting affinity chromatography ligands and scaffolds for combinatorial chemistry.
Conclusions:
- Affinity fingerprinting provides an efficient and quantitative approach to chemical space exploration and ligand identification.
- This method complements genomic target classification by providing ligand binding property insights.
- It offers a powerful tool for accelerating drug discovery and understanding protein-ligand interactions.
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