Privileged molecules for protein binding identified from NMR-based screening.

Hajduk PJ, Bures M, Praestgaard J, Fesik SW
J Med Chem. 2000 43 (18): 3443-7

PMID: 10978192 · DOI:10.1021/jm000164q

A statistical analysis of NMR-derived binding data on 11 protein targets was performed to identify molecular motifs that are preferred for protein binding. The analysis indicates that compounds which contain a biphenyl substructure preferentially bind to a wide range of proteins and that high levels of specificity (>250-fold) can be achieved even for these small molecules. These results suggest that high-throughput screening libraries that are enriched with biphenyl-containing compounds can be expected to have increased chances of yielding high-affinity ligands for proteins, and they suggest that the biphenyl can be utilized as a template for the discovery and design of therapeutics with high affinity and specificity for a broad range of protein targets.

MeSH Terms (8)

Biphenyl Compounds Databases, Factual Ligands Magnetic Resonance Spectroscopy Molecular Structure Protein Binding Proteins Structure-Activity Relationship

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