Abstract
[structure: see text] The C20 region of our bryostatin analogs was identified as a nonpharmacophoric site that could be varied to tune analogs for function and physical properties without significantly affecting their binding affinity for PKC. The use of this site in a late-stage diversification strategy has enabled the facile synthesis of a variety of new C20 analogs, all of which retain nanomolar affinity for PKC, in agreement with our pharmacophore hypothesis.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antineoplastic Agents / chemical synthesis*
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Antineoplastic Agents / chemistry*
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Brain / enzymology
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Bryostatins
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Clinical Trials, Phase I as Topic
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Clinical Trials, Phase II as Topic
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Macrolides / chemical synthesis*
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Macrolides / chemistry*
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Models, Molecular*
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Molecular Structure
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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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Antineoplastic Agents
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Bryostatins
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Macrolides
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bryostatin 1
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Protein Kinase C