Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Benzofurans / pharmacology
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Biological Products / pharmacology*
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Caffeic Acids / pharmacology
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Drug Discovery
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Humans
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Lactates / pharmacology
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Lymphocyte Specific Protein Tyrosine Kinase p56(lck) / antagonists & inhibitors
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Models, Molecular
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Phenols / pharmacology
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Protein Binding / drug effects
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Protein Kinase Inhibitors / pharmacology
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Proto-Oncogene Proteins pp60(c-src) / antagonists & inhibitors
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src Homology Domains / drug effects*
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src-Family Kinases / antagonists & inhibitors*
Substances
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Benzofurans
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Biological Products
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Caffeic Acids
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Lactates
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Phenols
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Protein Kinase Inhibitors
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salvianolic acid A
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salvianolic acid B
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Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
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Proto-Oncogene Proteins pp60(c-src)
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src-Family Kinases
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caftaric acid