1803-59-4

Basic information

• Product Name: Z-D-Leu-L-Ala-OCH₃
• Synonyms: Z-D-Leu-L-Ala-OCH₃
• CAS NO: 1803-59-4
• Molecular Weight: 350.415
• Mol File: 1803-59-4.mol
• Article Data: 12

Chemical Properties

• CAS DataBase Reference: Z-D-Leu-L-Ala-OCH₃(CAS DataBase Reference)
• NIST Chemistry Reference: Z-D-Leu-L-Ala-OCH₃(1803-59-4)
• EPA Substance Registry System: Z-D-Leu-L-Ala-OCH₃(1803-59-4)

Safety Data

• Hazardous Substances Data: 1803-59-4(Hazardous Substances Data)

Upstream product

• 7625-53-8 rac-Ala-OMe 
• 76863-45-1 (S)-benzyl (1-azido-4-methyl-1-oxopentan-2-yl)carbamate 
• 10065-72-2 L-Alanine methyl ester 
• 2018-66-8 Z-Leu-OH 
• 2491-20-5 L-alanine methyl ester hydrochloride 
• 28862-79-5 Z-D-Leu-OH 
• 1384344-98-2 Cbz-Leu-SH 
• 51021-87-5 N-benzyloxycarbonyl-L-leucine methyl ester 
• 501-53-1 benzyl chloroformate 
• 61-90-5 L-leucine 
• 125814-24-6 Z-Leu-NCA 
• 53363-87-4 N-(benzyloxycarbonyl)leucine dicyclohexylamine salt 

Downstream Products

• 126530-13-0 Z-Leu-Ala-Gly-NH₂ 
• 22209-80-9 Carbobenzoxy-Leu-D-Ala 
• 71447-64-8 Z-Leu-Ala-NHNH₂ 
• 2817-13-2 ((S)-2-(benzyloxycarbonylamino)-4-methylpentanamido)propanoic acid 
• 80189-14-6 Z-Leu-Ala-Leu-NH₂ 
• 87023-75-4 Z-Leu-Ala-Val-NH₂ 
• 19817-68-6 Z-Leu-Ala-OC₂H₅ 

Relevant articles and documents

Optimization and anti-cancer properties of fluoromethylketones as covalent inhibitors for ubiquitin C-terminal hydrolase L1

The deubiquitinating enzyme (DUB) UCHL1 is implicated in various disease states including neurodegenerative disease and cancer. However, there is a lack of quality probe molecules to gain a better understanding on UCHL1 biology. To this end a study was carried out to fully characterize and optimize the irreversible covalent UCHL1 inhibitor VAEFMK. Structure-activity relationship studies identified modifications to improve activity versus the target and a full cellular characterization was carried out for the first time with this scaffold. The studies produced a new inhibitor, 34, with an IC50 value of 7.7 μM against UCHL1 and no observable activity versus the closest related DUB UCHL3. The molecule was also capable of selectively inhibiting UCHL1 in cells and did not demonstrate any discernible off-target toxicity. Finally, the molecule was used for initial probe studies to assess the role of UCHL1 role in proliferation of myeloma cells and migration behavior in small cell lung cancer cells making 34 a new tool to be used in the biological evaluation of UCHL1.

Thioacetic acid/NaSH-mediated synthesis of N -protected amino thioacids and their utility in peptide synthesis

Thioacids are recently gaining momentum due to their versatile reactivity. The reactivity of thioacids has been widely explored in the selective amide/peptide bond formation. Thioacids are generally synthesized from the reaction between activated carboxylic acids such as acid chlorides, active esters, etc., and Na2S, H2S, or NaSH. We sought to investigate whether the versatile reactivity of the thioacids can be tuned for the conversion of carboxylic acids into corresponding thioacids in the presence of NaSH. Herein, we report that thioacetic acid- and NaSH-mediated synthesis of N-protected amino thioacids from the corresponding N-protected amino acids, oxidative dimerization of thioacids, crystal conformations of thioacid oxidative dimers, and the utility of thioacids and oxidative dimers in peptide synthesis. Our results suggest that peptides can be synthesized without using standard coupling agents.

An approach towards efficient peptide synthesis in aqueous solution

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