A switch in enantiomer preference between mitochondrial F 1F 0-ATPase chemotypes

The preferred absolute configuration of two series of F 1F 0-ATP synthase inhibitors was determined. Although the configuration of the active enantiomer in each series is different, each series presents the same ‘triaryl’ pharmacophore to the enzyme binding site. The preferred absolute configuration...

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Bibliographic Details
Published inBioorganic & medicinal chemistry letters Vol. 15; no. 11; pp. 2749 - 2751
Main Authors Bisaha, Sharon N., Malley, Mary F., Pudzianowski, Andrew, Monshizadegan, Hossain, Wang, Paulina, Madsen, Cort S., Gougoutas, Jack Z., Stein, Philip D.
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 2005
Subjects
Acylguanidine
Chiral synthesis
Mitochondrial ATPase
Acylguanidine
Chiral synthesis
Mitochondrial ATPase
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Summary:The preferred absolute configuration of two series of F 1F 0-ATP synthase inhibitors was determined. Although the configuration of the active enantiomer in each series is different, each series presents the same ‘triaryl’ pharmacophore to the enzyme binding site. The preferred absolute configuration of two series of F 1F 0-ATP synthase inhibitors was determined. Although the configuration of the active enantiomer in each series is different, each series presents the same ‘triaryl’ pharmacophore to the enzyme binding site.
ISSN:0960-894X
1464-3405
DOI:10.1016/j.bmcl.2005.03.115