118252-77-0Relevant academic research and scientific papers
Facile synthesis of optically active imidazole derivatives
Marek, Ales,Kulhanek, Jiri,Ludwig, Miroslav,Bures, Filip
, p. 1183 - 1190 (2008/02/07)
Five optically active imidazole derivatives have been synthesized via a facile 4-step reaction sequence starting from commercially available and inexpensive N-Cbz amino acids. While microwave assisted condensation was unsuccessful, the condensation of the
Chiral imidazole derivatives synthesis from enantiopure N-protected α-amino acids
Bures, Filip,Kulhanek, Jiri
, p. 1347 - 1354 (2007/10/03)
A route to the preparation of enantiopure ligands based on a 2-phenylimidazol ring is described. The stereogenic centre is placed into the chain bonded to the fourth carbon of the imidazole ring. The synthesis starts from inexpensive and readily available
Stereocontrolled synthesis of erythro N-protected α-amino epoxides and peptidyl epoxides
Albeck, Amnon,Persky, Rachel
, p. 6333 - 6346 (2007/10/02)
N-protected α-amino epoxides of erythro configuration, derived from α-amino acids, were synthesized in a stereoselective manner. The erythro (2S,3S), configuration was achieved by the synthetic sequence: amino acid -> haloketone -> halohydrin -> epoxide. A mechanistic explanation for the observed stereoselectivity is presented. This stereoselective synthetic approach was applied to the synthesis of a variety of short peptidyl epoxides, bearing a predefined absolute configuration of the chiral epoxide moiety.
Renin inhibitors containing isosteric replacements of the amide bond connecting the P3 and P2 sites
Kaltenbronn,Hudspeth,Lunney,Michniewicz,Nicolaides,Repine,Roark,Stier,Tinney,Woo,Essenburg
, p. 838 - 845 (2007/10/02)
Renin inhibitors having 13 different isosteres connecting the P3 and P2 positions have been prepared. Synthetic routes and in vitro activity exhibited by these compounds are discussed. The two most potent compounds, 47 and 48, contai
Inhibition of aminopeptidases by peptides containing ketomethylene and hydroxyethylene amide bond replacements
Harbeson,Rich
, p. 1378 - 1392 (2007/10/02)
Inhibitors of aminopeptidase enzymes have been prepared by the synthesis of peptide substrate analogues in which the scissile amide bond has been replaced with the hydrolytically stable ketomethylene (-COCH2-) and hydroxyethylene [-CH(OH)CHsub
