1-(5-Carboxyindazol-1-yl)propan-2-ones as dual inhibitors of cytosolic phospholipase A2α and fatty acid amide hydrolase: bioisosteric replacement of the carboxylic acid moiety

doi:10.1080/14756366.2016.1178246

Paper

1-(5-Carboxyindazol-1-yl)propan-2-ones as dual inhibitors of cytosolic phospholipase A2α and fatty acid amide hydrolase: bioisosteric replacement of the carboxylic acid moiety

Published May 9, 2016 · J. Althaus, Theresa Hake, Walburga Hanekamp

Journal of Enzyme Inhibition and Medicinal Chemistry

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6

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Abstract

Abstract Indazole-5-carboxylic acids with 3-aryloxy-2-oxopropyl residues in position 1 were previously reported to be potent dual inhibitors of cytosolic phospholipase A2α (cPLA2α) and fatty acid amide hydrolase (FAAH). In continuation of our structure-activity studies on cPLA2α and FAAH inhibitors, a number of derivatives of these substances characterized by bioisosteric replacement of the carboxylic acid functionality by inverse amides, sulfonylamides, carbamates and ureas were prepared. The biological evaluation of the obtained compounds showed that the carboxylic acid functionality of the lead compounds is of special importance for a pronounced inhibition of cPLA2α and FAAH.

In Vitro Study

Study Snapshot

Indazole-5-carboxylic acids with 3-aryloxy-2-oxopropyl residues in position 1 are potent dual inhibitors of cytosolic phospholipase A2 and fatty acid amide hydrolase, with the carboxylic acid functionality being crucial for pronounced

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

1-(5-Carboxyindazol-1-yl)propan-2-ones as dual inhibitors of cytosolic phospholipase A2α and fatty acid amide hydrolase: bioisosteric replacement of the carboxylic acid moiety

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