Abstract
4-benzylquinolines 5, based on a series of isoquinolines 1, were prepared and tested as inhibitors of the IGF/IGFBP-3 complex based on their ability to displace IGF-I from its binding to IGF-binding protein-3. SAR studies on the 6,7-dihydroxy moiety of the quinoline 5a showed that the catecol moiety could be replaced with other functional groups. Computational modeling of the 5a/mini-IGFBP-5 complex revealed the possible binding site of 5a on IGFBP-5.
MeSH terms
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Acids, Carbocyclic / chemistry*
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Acids, Carbocyclic / pharmacology*
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Amino Acid Sequence
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Binding Sites
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Binding, Competitive
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Humans
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Insulin-Like Growth Factor Binding Protein 3 / antagonists & inhibitors*
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Insulin-Like Growth Factor Binding Protein 3 / genetics
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Insulin-Like Growth Factor Binding Protein 3 / metabolism
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Insulin-Like Growth Factor Binding Protein 5 / genetics
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Insulin-Like Growth Factor Binding Protein 5 / metabolism
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Insulin-Like Growth Factor I / antagonists & inhibitors*
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Insulin-Like Growth Factor I / metabolism
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Models, Molecular
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Molecular Sequence Data
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Quinolines / chemical synthesis
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Quinolines / chemistry*
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Quinolines / pharmacology*
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Structure-Activity Relationship
Substances
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Acids, Carbocyclic
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Insulin-Like Growth Factor Binding Protein 3
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Insulin-Like Growth Factor Binding Protein 5
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Quinolines
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Insulin-Like Growth Factor I