438044-70-3

Upstream product

• 1256776-41-6 1-((1-hydroxy-4-phenylbutan-2-ylcarbamoyl)-3-methylbutyl)morpholine-4-carboxamide 
• 1256776-38-1 2-(4-methyl-2-(morpholine-4-carboxamido)pentanoylamino)-4-phenylbutanoic acid methyl ester 
• 294885-32-8 2S-amino-N-methoxy-N-methyl-4-phenyl-butyramide 
• 129739-09-9 4-methyl-2S-[(morpholine-4-carbonyl)amino]pentanoic acid 
• 438044-95-2 Morpholine-4-carboxylic acid {(S)-1-[(S)-1-(methoxy-methyl-carbamoyl)-3-phenyl-propylcarbamoyl]-3-methyl-butyl}-amide 

Downstream Products

• 900813-43-6 Morpholine-4-carboxylic acid {(S)-1-[(S)-1-(benzoyl-hydrazonomethyl)-3-phenyl-propylcarbamoyl]-3-methyl-butyl}-amide 
• 1256776-27-8 C₃₁H₄₅N₃O₆ 

Relevant academic research and scientific papers

Endoperoxide carbonyl falcipain 2/3 inhibitor hybrids: Toward combination chemotherapy of malaria through a single chemical entity

We extend our approach of combination chemotherapy through a single prodrug entity (O'Neill et al. Angew. Chem., Int. Ed. 2004, 43, 4193) by using a 1,2,4-trioxolane as a protease inhibitor carbonyl-masking group. These molecules are designed to target the malaria parasite through two independent mechanisms of action: iron(II) decomposition releases the carbonyl protease inhibitor and potentially cytotoxic C-radical species in tandem. Using a proposed target "heme", we also demonstrate heme alkylation/carbonyl inhibitor release and quantitatively measure endoperoxide turnover in parasitized red blood cells.

The design of potent hydrazones and disulfides as cathepsin S inhibitors

The design and synthesis of dipeptidyl disulfides and dipeptidyl benzoylhydrazones as selective inhibitors of the cysteine protease Cathepsin S are described. These inhibitors were expected to form a slowly reversible covalent adduct of the active site cysteine of Cathepsin S. Formation of the initial adduct was confirmed by mass spectral analysis. The nature and mechanism of these adducts was explored. Kinetic analysis of the benzoyl hydrazones indicate that these inhibitors are acting as irreversible inhibitors of Cathepsin S. Additionally, the benzoylhydrazones were shown to be potent inhibitors of Cathepsin S processing of Class II associated invariant peptide both in vitro and in vivo.