A switch in enantiomer preference between mitochondrial F1F0-ATPase chemotypes

Sharon N Bisaha; Mary F Malley; Andrew Pudzianowski; Hossain Monshizadegan; Paulina Wang; Cort S Madsen; Jack Z Gougoutas; Philip D Stein

doi:10.1016/j.bmcl.2005.03.115

A switch in enantiomer preference between mitochondrial F1F0-ATPase chemotypes

Bioorg Med Chem Lett. 2005 Jun 2;15(11):2749-51. doi: 10.1016/j.bmcl.2005.03.115.

Authors

Sharon N Bisaha¹, Mary F Malley, Andrew Pudzianowski, Hossain Monshizadegan, Paulina Wang, Cort S Madsen, Jack Z Gougoutas, Philip D Stein

Affiliation

¹ Department of Discovery Chemistry, Bristol-Myers Squibb, Pharmaceutical Research Institute, Princeton, NJ 08543-4000, USA.

PMID: 15878269
DOI: 10.1016/j.bmcl.2005.03.115

Abstract

The preferred absolute configuration of two series of F(1)F(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.

MeSH terms

Binding Sites
Mitochondria / enzymology*
Models, Molecular
Proton-Translocating ATPases / metabolism*
Stereoisomerism

Substances

Proton-Translocating ATPases