A switch in enantiomer preference between mitochondrial F1F0-ATPase chemotypes.
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.
Bisaha
Sharon N
SN
Department of Discovery Chemistry, Bristol-Myers Squibb, Pharmaceutical Research Institute, Princeton, NJ 08543-4000, USA.
Malley
Mary F
MF
Pudzianowski
Andrew
A
Monshizadegan
Hossain
H
Wang
Paulina
P
Madsen
Cort S
CS
Gougoutas
Jack Z
JZ
Stein
Philip D
PD
D001665:Binding Sites; D008928:Mitochondria / Q000201:enzymology*; D008958:Models, Molecular; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013237:Stereoisomerism
D006180:Proton-Translocating ATPases