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J Med Chem. 2001 Dec 6;44(25):4309-12.

Conformationally constrained analogues of diacylglycerol. 18. The incorporation of a hydroxamate moiety into diacylglycerol-lactones reduces lipophilicity and helps discriminate between sn-1 and sn-2 binding modes to protein kinase C (PK-C). Implications for isozyme specificity.

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1
Laboratory of Medicinal Chemistry, College of Pharmacy, Seoul National University, Shinlin Dong, Kwanak-ku, Seoul 151-742, South Korea. jeewoo@snu.ac.kr

Erratum in

  • J Med Chem. 2003 Jun 19;46(13):2794.

Abstract

An approach to reduce the log P in a series of diacylglycerol (DAG)-lactones known for their high binding affinity for protein kinase C (PK-C) is presented. Branched alkyl groups with reduced lipophilicity were selected and combined with the replacement of the ester or lactone oxygens by NH or NOH groups. Compound 6a with an isosteric N-hydroxyl amide arm represents the most potent and least lipophilic DAG analogue known to date.

PMID:
11728178
DOI:
10.1021/jm0103965
[Indexed for MEDLINE]

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