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Bioorg Med Chem Lett. 2008 May 15;18(10):3043-6. doi: 10.1016/j.bmcl.2008.01.002. Epub 2008 Jan 8.

Synthesis and stereochemistry of the terminal spiroketal domain of the phosphatase inhibitor dinophysistoxin-2.

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1
Department of Chemistry, The Ohio State University, 100 W. 18th Avenue, Columbus, OH 43210, USA. forsyth@chemistry.ohio-state.edu

Abstract

An expedient synthesis of both axially and equatorially C35 methyl substituted spiroketals representing the C28-C38 domain of the potent and selective protein serine/threonine phosphatase inhibitor dinophysistoxin-2 (DTX-2) was developed to enable comparative stereochemical analyses and a stereochemically correct total synthesis of DTX-2. Comparison of proton and carbon NMR data of the synthetic diastereomers with those published for DTX-2 indicates that DTX-2 possesses the (30S *,34R *,35S *)-relative configuration with an axial C35 methyl substituent.

PMID:
18226903
DOI:
10.1016/j.bmcl.2008.01.002
[Indexed for MEDLINE]
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