Natural product inhibitors of protein–protein interactions mediated by Src-family SH2 domains

In this Letter, we report the natural products salvianolic acid A, salvianolic acid B, and caftaric acid as inhibitors of the protein–protein interactions mediated by the SH2 domains of the Src-family kinases Src and Lck, two established disease targets. Moreover, we propose a binding mode for the i...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 2009-06, Vol.19 (12), p.3305-3309
Main Authors: Sperl, Bianca, Seifert, Markus H.J., Berg, Thorsten
Format: Article
Language:English
Subjects:
Benzofurans - pharmacology
Biological and medical sciences
Biological Products - pharmacology
Caffeic Acids - pharmacology
Drug Discovery
Humans
Lactates - pharmacology
Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - antagonists & inhibitors
Medical sciences
Miscellaneous
Models, Molecular
Pharmacology. Drug treatments
Phenols - pharmacology
Protein Binding - drug effects
Protein Kinase Inhibitors - pharmacology
Proto-Oncogene Proteins pp60(c-src) - antagonists & inhibitors
src Homology Domains - drug effects
src-Family Kinases - antagonists & inhibitors
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Summary:In this Letter, we report the natural products salvianolic acid A, salvianolic acid B, and caftaric acid as inhibitors of the protein–protein interactions mediated by the SH2 domains of the Src-family kinases Src and Lck, two established disease targets. Moreover, we propose a binding mode for the inhibitors based on molecular modeling, which will facilitate chemical optimization efforts of these important lead structures for drug discovery.
ISSN:0960-894X
1464-3405
DOI:10.1016/j.bmcl.2009.04.083