18598-66-8

Upstream product

• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 76-83-5 trityl chloride 
• 2666-93-5 (S)-Leu-OMe 
• 61-90-5 L-leucine 

Downstream Products

• 100841-17-6 4-methyl-2(S)-<(triphenylmethyl)amino>-1-pentanol 
• 123381-26-0 (2S,3S)-dimethyl <2-hydroxy-5-methyl-3-(tritylamino)hexyl>phosphonate 
• 153451-35-5 N-trityl-3-methyl-1-vinyl-butylamine 
• 647852-12-8 (E)-(S)-6-Methyl-1-phenyl-4-(trityl-amino)-hept-1-en-3-one 
• 647852-20-8 (S)-5-Methyl-2-oxo-3-(trityl-amino)-hexanoic acid methyl ester 
• 647852-27-5 (2S,3S)-3-Benzoylamino-2-hydroxy-5-methyl-hexanoic acid methyl ester 
• 257296-69-8 methyl (4S,trans)-4,5-dihydro-2-isobutyl-4-phenyl-5-carboxylate 

Relevant academic research and scientific papers

Double chirality transmission in trityl amines: Sensing molecular dynamic stereochemistry by circular dichroism and DFT calculations

Con-figured out: The tert-butyl group can be formally seen as "less" sterically demanding (M) than the methyl group (L). This is the case when a CD-active trityl group at the nitrogen atom is used to report the chirality of the carbon substituent with two

A practical diastereoselective synthesis of β-amino-α-hydroxy carboxylates

Practical synthetic routes to β-amino-α-hydroxy carboxylates (AHC) have been developed from amino acids. Reduction of β-amino-α- keto esters 6 with NaBH4 was found to give anti-AHCs 7 in high de, which were efficiently converted to the corresponding syn-AHCs 8 via oxazolidine ring 10 formation.

New inhibitors of renin that contain novel phosphostatine Leu-Val replacements

A novel series of renin inhibitors based on the Phe8-His9-Leu10-Val11 substructure of renin's natural substrate, angiotensinogen, is reported. These inhibitors retain the Phe8-His9 portion of the native substructure and employ novel phosphostatine Leu10-Val11 replacements (LVRs). The phosphostatine LVRs were prepared by condensing a dialkyl phosphonate ester stabilized anion with either N-t-Boc-amino aldehydes or N-tritylamino aldehydes (derived from the corresponding amino acid). Structure-activity relationships at the Leu10 side chain revealed that the LVR derived from L-cyclohexylalanine provided a 130-fold boost in potency over the LVR derived from L-leucine. The dialkyl ester moiety was varied and a loss in potency was incurred when the alkyl ester was chain extended or α-branced; dimethyl esters provided optimum potency. The phosphonate moiety was replaced by a half-acid half-ester phosphonate and dimethylphosphinate; both replacements lead to a loss in potency. The more potent inhibitors (IC50 = 20-50 nM) were found to be selective inhibitors for renin over porcine pepsin and bovine cathepsin D (little or no inhibition was observed at 10-5 M).