179015-36-2

Upstream product

• 171514-07-1 (+)-2-acetamido-3-azidopropanoic acid methyl ester 
• 130106-12-6 Methyl-2(S)-benzyloxycarbonylamino-3-acetylamino-propionate 

Downstream Products

• 1482-97-9 (S)-2,3-diaminopropanoic acid hydrochloride 
• 199005-55-5 {(S)-1-[(S)-1-((S)-2-Acetylamino-1-formyl-ethylcarbamoyl)-2-phenyl-ethylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester 
• 199005-54-4 {(S)-1-[(S)-1-((S)-2-Acetylamino-1-hydroxymethyl-ethylcarbamoyl)-2-phenyl-ethylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester 

Relevant academic research and scientific papers

Synthesis, activity and structure-activity relationship of noroviral protease inhibitors

The protease of norovirus, an important human pathogen, is essential for the viral replication and, therefore, represents a potential drug target. A series of tripeptide-based inhibitors of the protease were designed, synthesized and tested, among which several potent inhibitors were identified with K i values as low as 75 nM. The structure-activity relationships of these inhibitors are discussed.

Inhibitors of farnesyl-protein transferase

The present invention comprises analogs of the CAAX motif of the protein Ras that is modified by farnesylation in vivo. These CAAX analogs inhibit farnesyl-protein transferase. Furthermore, these CAAX analogues differ from those previously described as inhibitors of farnesyl-protein transferase in that they do not have a thiol moiety. The lack of the thiol offers unique advantages in terms of improved pharmacokinetic behavior in animals, prevention of thiol-dependent chemical reactions, such as rapid autoxidation and disulfide formation with endogenous thiols, and reduced systemic toxicity. Further contained in this invention are chemotherapeutic compositions containing these farnesyl transferase inhibitors and methods for their production.

Inhibitors of farnesyl-protein transferase

The present invention comprises analogs of the CA1 A2 X motif of the protein Ras that is modified by farnesylation in vivo. These CA1 A2 X analogs inhibit the farnesyl-protein transferase and the farnesylation of certain proteins. Furthermore, these CA1 A2 X analogs differ from those previously described as inhibitors of farnesyl-protein transferase in that they do not have a thiol moiety. The lack of the thiol offers unique advantages in terms of improved pharmacokinetic behavior in animals, prevention of thiol-dependent chemical reactions, such as rapid autoxidation and disulfide formation with endogenous thiols, and reduced systemic toxicity. The compounds of the instant invention also incorporate a cyclic amine moiety in the A2 position of the motif. Further contained in this invention are chemotherapeutic compositions containing these farnesyl transferase inhibitors and methods for their production.

INHIBITORS OF FARNESYL-PROTEIN TRANSFERASE

The present invention comprises analogs of the CAAX motif of the protein Ras that is modified by farnesylation in vivo. These CAAX analogs inhibit farnesyl-protein transferase. Furthermore, these CAAX analogues differ from those previously described as inhibitors of farnesyl-protein transferase in that they do not have a thiol moiety. The lack of the thiol offers unique advantages in terms of improved pharmacokinetic behavior in animals, prevention of thiol-dependent chemical reactions, such as rapid antoxidation and disulfide formation with endogenous thiols, and reduced systemic toxicity. Further contained in this invention are chemotherapeutic compositions containing these farnesyl transferase inhibitors and methods for their production.

Stereochemistry of Nucleophilic Ring-Opening Reactions of Optically Active N-Acetyl-2-Methoxycarbonylaziridine.

The SN2-like mechanism of the nucleophilic attack of sodium azide on (S)-(-)-N-acetyl-2-methoxycarbonylaziridine was verified through the chemical correlation of the ring-opening products with (S)-(+)- or (R)-(-)-2,3-diaminopropanoic acid monohydrochloride.