117499-02-2Relevant academic research and scientific papers
Potent and Selective Inhibitors of an Aspartyl Protease-like Endothelin Converting Enzyme Identified in Rat Lung
Shiosaki, Kazumi,Tasker, Andrew S.,Sullivan, Gerard M.,Sorensen, Bryan K.,Geldern, Thomas W. von,et al.
, p. 468 - 478 (2007/10/02)
Two structurally distinct series of potent and selective inhibitors of an aspartyl protease-like endothelin converting enzyme (ECE) activity identified in the rat lung have been developed.Pepstatin A, which potently inhibits the rat lung ECE, served as the basis for the first series.Alternatively, selected renin inhibitors containing the dihydroxyethylene moiety were shown to be inhibitors of rat lung activity.Subsequent modifications improved inhibition of the rat lung ECE while eliminating renin activity.Both series of ECE inhibitors demonstrated a range of selectivity over Cathepsin D.Water-solubilizing moieties were appended onto selected compounds to facilitate in vivo testing.Partial reduction of the pressor response to exogenously administered Big ET-1 was observed with selected rat lung ECE inhibitors.
Unique Stereocontrol in Europium (III)-Catalyzed Cyanosilylation of chiral α-Alkoxy and α-Amino Aldehydes
Gu, Jin-Hua,Okamoto, Mikako,Terada, Masahiro,Mikami, Koichi,Nakai, Takeshi
, p. 1169 - 1172 (2007/10/02)
The Eu(III)-catalyzed cyanosilylations of chiral α-alkoxy and α-amino aldehydes are shown to exhibit syn diastereofacial selection, the degree increasing with an increase in steric bulk of the alkyl chain in the aldehydes.The mechanism of this catalytic p
