Abstract
The syntheses of three newly designed bryostatin analogues are reported. These simplified analogues, which lack the A-ring present in the natural product but possess differing groups at C9, were obtained using a divergent approach from a common intermediate. All three analogues exhibit potent, single-digit nanomolar affinity to protein kinase C.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Binding Sites
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Brain / enzymology
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Bryostatins
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Macrolides / chemical synthesis*
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Macrolides / chemistry*
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Macrolides / pharmacology
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Molecular Structure
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Protein Kinase C / chemistry*
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Protein Kinase C / metabolism
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Rats
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Structure-Activity Relationship
Substances
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Bryostatins
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Macrolides
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bryostatin 1
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Protein Kinase C