2483-52-5

Upstream product

• 78814-79-6 N-(N-benzyloxycarbonyl-D-alanyl)-L-alanine ethyl ester 
• 19914-27-3 N-benzyloxycarbonyl-D-alaninyl-L-alanine methyl ester 
• 57355-13-2 N-benzyloxycarbonylalaninehydrazid 
• 26607-51-2 N-benzyloxycarbonyl-D-alanine 
• 5673-69-8 N-benzyloxycarbonyl-L-alanyl-L-alanine ethyl ester 
• 2483-51-4 N-[(benzyloxy)carbonyl]-L-alanyl-L-alanine methyl ester 
• 17350-66-2 N-benzyloxycarbonylalaninehydrazid 
• 79411-36-2 Z-D-Ala-D-Ala-OEt 
• 64532-72-5 Z-L-Ala-D-Ala-OEt 
• 1142-20-7 N-Cbz-Ala 

Downstream Products

• 907564-30-1 N-[N-(N-benzyloxycarbonyl-D-alanyl)-L-alanyl]-L-alanine benzyl ester 
• 5673-67-6 N-benzyloxycarbonyl-L-alanyl-L-alanyl-L-alanine ethyl ester 
• 90427-70-6 Cbz-L-ala-L-ala-L-ala-Cbz 
• 5673-67-6 N-[N-(N-benzyloxycarbonyl-L-alanyl)-L-alanyl]-D-alanine ethyl ester 
• 70462-22-5 N-[N-(N-benzyloxycarbonyl-L-alanyl)-L-alanyl]-D-alanine benzyl ester 
• 52357-40-1 Z-Ala-Ala-Ala-pNA 
• 84914-63-6 Benzyloxycarbonylalanyl-alanyl-proline Ethylamide 
• 646532-75-4 N¹-(N-benzyloxycarbonylalanylalanyl)-N²-ethoxycarbonylmethylhydrazine 
• 60354-61-2 L-Ala-L-Ala-L-Ala-pNA 
• 52299-14-6 N-succinyl-L-alanyl-L-alanyl-L-alanine 4-nitroanilide 
• 83808-37-1 4-{(S)-1-[(S)-2-((S)-2-Ethylcarbamoyl-pyrrolidin-1-yl)-1-methyl-2-oxo-ethylcarbamoyl]-ethylcarbamoyl}-butyric acid 
• 3245-67-8 N-[N-(N-benzyloxycarbonyl-L-alanyl)-L-alanyl]-D-alanine hydrazide 
• 82748-61-6 N-[N-(N-benzyloxycarbonyl-L-alanyl)-L-alanyl]-L-alanine hydrazide 
• 903510-11-2 N-[N-(N-benzyloxycarbonyl-D-alanyl)-D-alanyl]-D-alanine benzyl ester 

Relevant academic research and scientific papers

Design, synthesis, and in vitro evaluation of aza-peptide aldehydes and ketones as novel and selective protease inhibitors

Aza-peptide aldehydes and ketones are a new class of reversible protease inhibitors that are specific for the proteasome and clan CD cysteine proteases. We designed and synthesised aza-Leu derivatives that were specific for the chymotrypsin-like active si

AZA-PEPTIDE ALDEHYDES AND KETONES

The present disclosure relates to compositions for inhibiting proteases, methods for synthesizing the compositions, and methods of using the disclosed protease inhibitors. Aspects of the invention include aza-peptide aldehyde and ketone compositions that inhibit proteases. The disclosed compounds, pharmaceutically acceptable salts, pharmaceutically acceptable derivatives, prodrugs, or combinations thereof can be used to treat disease or pathological conditions related to the activity of proteases associated with a specific disease or condition.

Aza-peptidyl Michael acceptors. A new class of potent and selective inhibitors of asparaginyl endopeptidases (legumains) from evolutionarily diverse pathogens

Aza-peptide Michael acceptors with the general structure of Cbz-Ala-Ala-AAsn-trans-CH=CHCOR are a new class of inhibitors specific for the asparaginyl endopeptidases (AE) (legumains). Structure-activity relationships (SARs) were characterized for a set of 31 aza-peptide Michael acceptors with AEs derived from three medically important parasites: the protist Trichomonas vaginalis, the hard tick Ixodes ricinus, and the flatworm Schistosoma mansoni. Despite arising from phylogenetically disparate organisms, all three AEs shared a remarkably similar SAR with lowest IC50 values extending into the picomolar range. The results suggest an evolutionary constraint on the topography of the prime side of the active site. SAR also revealed that esters in the P1′ position are more potent than disubstituted amides and that monosubstituted amides and alkyl derivatives show little or no inhibition. The preferred P1′ residues have aromatic substituents. Aza-asparaginyl Michael acceptors react with thiols, which provides insight into the mechanism of their inhibition of asparaginyl endopeptidases.

Aza-Peptide Michael Acceptors: A New Class of Inhibitors Specific for Caspases and Other Clan CD Cysteine Proteases

Aza-peptide Michael acceptors are a new class of irreversible inhibitors that are highly potent and specific for clan CD cysteine proteases. The aza-Asp derivatives were specific for caspases, while aza-Asn derivatives were effective legumain inhibitors. Aza-Lys and aza-Orn derivatives were potent inhibitors of gingipain K and clostripain. Aza-peptide Michael acceptors showed no cross reactivity toward papain, cathepsin B, and calpain.

Aza-peptide epoxides: A new class of inhibitors selective for clan CD cysteine proteases

Aza-peptide epoxides, a new class of irreversible protease inhibitors, are specific for the clan CD cysteine proteases. The inhibitors have second-order rate constants up to 105 M-1 s-1, with the most potent epoxides having the S,S stereochemistry. The aza-Asn derivatives are effective legumain inhibitors, while the aza-Asp epoxides were specific for caspases. The inhibitors have little or no inhibition with other proteases such as chymotrypsin, papain, or cathepsin B.