135674-98-5

Upstream product

• 61070-20-0 N^α-(tert-butoxycarbony1)- N^τ-methyl-L-histidine 
• 122225-24-5 (1'R,2'S,5S)-5-(2'-amino-3'-cyclohexyl-1'-hydroxypropyl)-3-ethyloxazolidin-2-one 

Downstream Products

• 1053255-26-7 {2-[(S)-1-{(S)-1-[(1S,2R)-1-Cyclohexylmethyl-2-((S)-3-ethyl-2-oxo-oxazolidin-5-yl)-2-hydroxy-ethylcarbamoyl]-2-thiophen-2-yl-ethylcarbamoyl}-2-(4-methoxy-phenyl)-ethylcarbamoyl]-1,1-dimethyl-ethyl}-carbamic acid tert-butyl ester 
• 131067-26-0 (R)-2-Benzyl-N-[(S)-1-[(1S,2R)-1-cyclohexylmethyl-2-((S)-3-ethyl-2-oxo-oxazolidin-5-yl)-2-hydroxy-ethylcarbamoyl]-2-(1-methyl-1H-imidazol-4-yl)-ethyl]-4-morpholin-4-yl-4-oxo-butyramide 
• 122225-00-7 (R)-2-Benzyl-N-{(S)-1-[(1S,2R)-1-cyclohexylmethyl-2-((S)-3-ethyl-2-oxo-oxazolidin-5-yl)-2-hydroxy-ethylcarbamoyl]-2-thiophen-2-yl-ethyl}-4-morpholin-4-yl-4-oxo-butyramide 

Relevant academic research and scientific papers

Studies directed toward the design of orally active renin inhibitors. 1. Some factors influencing the absorption of small peptides

A systematic evaluation of structure-absorption relationships using a high throughput intraduodenal rat screening model has led to the delineation of a set of structural parameters that appear to govern bioavailability in a series of peptide-based renin inhibitors. Optimum structures, exemplified by 25 and 41, incorporated a single, solubilizing substituent at the C- or N- terminus combined with a lipophilic P2-site residue. Both inhibitors gave unprecedented plasma drug levels upon intraduodenal administration to monkeys, and the calculated bioavailability for 41 (14 ± 4%) is the highest reported for any peptidic renin inhibitor.