2817-13-2

Usage

Uses

Used in Pharmaceutical Research:
Z-L-LEUCYL-L-ALANINE is used as a research compound for investigating its potential biological activities, including antimicrobial and anticancer properties. Its inhibitory effects on enzymes such as trypsin and chymotrypsin make it a valuable tool for understanding enzyme functions and developing new therapeutic agents.
Used in Biochemical Research:
Z-L-LEUCYL-L-ALANINE is used as a synthetic dipeptide for studying peptide interactions and functions in biological systems. Its antioxidant and anti-inflammatory properties provide insights into the development of novel therapeutic approaches for various diseases.
Used in Drug Development:
Z-L-LEUCYL-L-ALANINE is used as a potential therapeutic agent for its antimicrobial and anticancer properties. Its ability to inhibit enzyme activity and exhibit antioxidant and anti-inflammatory effects makes it a promising candidate for the development of new drugs targeting various diseases.
Used in Enzyme Inhibition Studies:
Z-L-LEUCYL-L-ALANINE is used as an enzyme inhibitor for studying the activity of enzymes such as trypsin and chymotrypsin. Its inhibitory effects on these enzymes contribute to a better understanding of enzyme functions and the development of enzyme-targeted therapies.
Used in Antioxidant and Anti-inflammatory Research:
Z-L-LEUCYL-L-ALANINE is used as a compound with potential antioxidant and anti-inflammatory properties. Its ability to exhibit these effects can provide insights into the development of novel therapeutic agents for diseases associated with oxidative stress and inflammation.

InChI:InChI=1/C17H24N2O5/c1-11(2)9-14(15(20)18-12(3)16(21)22)19-17(23)24-10-13-7-5-4-6-8-13/h4-8,11-12,14H,9-10H2,1-3H3,(H,18,20)(H,19,23)(H,21,22)/t12-,14-/m0/s1

Upstream product

• 56-41-7 L-alanin 
• 102156-97-8 N-benzyloxycarbonyl-L-thioleucine S-phenyl ester 
• 1803-59-4 N-benzyloxycarbonyl-L-leucyl-L-alanine methyl ester 
• 7797-39-9 Z-L-Leucin-<5-chlor-chinolyl-(8)-ester> 
• 910902-20-4 N-Benzyloxycarbonyl-L-leucin-<1-selenonaphthyl>-ester 
• 53481-48-4 (S)-tert-butyl 2-((S)-2-(benzyloxycarbonylamino)-4-methylpentanamido)propanoate 
• 2018-66-8 Z-Leu-OH 

Downstream Products

• 7298-84-2 Leu-Ala 
• 113798-67-7 {(S)-1-[(S)-1-(6-Methoxy-quinolin-8-ylcarbamoyl)-ethylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester 
• 115572-33-3 ethyl benzyloxycarbonylleucyl-alanyl-1-amino-1-cyclopentanecarboxylate 
• 203053-79-6 (S)-1-[(S)-2-((S)-2-Benzyloxycarbonylamino-4-methyl-pentanoylamino)-propionyl]-pyrrolidine-2-carboxylic acid 2-trimethylsilanyl-ethyl ester 
• 1027731-06-1 (E)-(S)-4-[(S)-2-((S)-2-Benzyloxycarbonylamino-4-methyl-pentanoylamino)-propionylamino]-6-(trityl-carbamoyl)-hex-2-enoic acid ethyl ester 
• 148334-80-9 [(S)-1-((S)-3-Diazo-1-methyl-2-oxo-propylcarbamoyl)-3-methyl-butyl]-carbamic acid benzyl ester 
• 244021-38-3 benzyl ((S)-1-(((S)-1-(methoxy(methyl)amino)-1-oxopropan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)carbamate 
• 1449017-99-5 C₂₃H₃₃N₃O₆ 
• 1449017-98-4 C₂₃H₃₄N₂O₅ 
• 126306-95-4 Diphenyl-N-(benzyloxycarbonyl)-L-leucyl-(2-decarboxy-L-alanin-2-yl)phosphonat 

Relevant academic research and scientific papers

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.

Exploring Structural Determinants of Inhibitor Affinity and Selectivity in Complexes with Histone Deacetylase 6

Inhibition of histone deacetylase 6 (HDAC6) has emerged as a promising therapeutic strategy for the treatment of cancer, chemotherapy-induced peripheral neuropathy, and neurodegenerative disease. The recent X-ray crystal structure determination of HDAC6 enables an understanding of structural features directing affinity and selectivity in the active site. Here, we present the X-ray crystal structures of five HDAC6-inhibitor complexes that illuminate key molecular features of the inhibitor linker and capping groups that facilitate and differentiate binding to HDAC6. In particular, aromatic and heteroaromatic linkers nestle within an aromatic cleft defined by F583 and F643, and different aromatic linkers direct the capping group toward shallow pockets defined by the L1 loop, the L2 loop, or somewhere in between these pockets. These results expand our understanding of factors contributing to the selective inhibition of HDAC6, particularly regarding interactions that can be targeted in the region of the L2 pocket.

Peptidyl allyl sulfones: A new class of inhibitors for clan CA cysteine proteases

A new series of peptidyl allyl sulfone inhibitors was discovered while trying to synthesize epoxy sulfone inhibitors from vinyl sulfones using basic oxidizing conditions. The various dipeptidyl allyl sulfones were evaluated with calpain I, papain, cathepsins B and L, cruzain and rhodesain and found to be potent inhibitors. In comparison to the previously developed class of vinyl sulfone inhibitors, the novel dipeptidyl allyl sulfones were more potent inhibitors than the corresponding dipeptidyl vinyl sulfones. It was observed that the stereochemistry of the vinyl sulfone precursor played a role in the potency of the dipeptidyl allyl sulfone inhibitor.

PEPTIDE SYNTHESIS CATALYZED BY NATIVE PROTEINASE K IN WATER-MISCIBLE ORGANIC SOLVENTS WITH LOW WATER CONTENT

Rection of Ac-Tyr-OEt with HBr.Gly-NH2, catalysed by free proteinase K in various water-miscible organic solvents in the presence of triethylamine and 5 mol percent of water, was studied.Some aliphatic alcohols and acetonitrile proved to be suitable solvents.The effect of water content (2 percent - 20 percent) on the synthesis of Ac-Tyr-Gly-NH2 was studied using acetonitrile as solvent.Lowering of the water content to 5 percent or 2 percent led to almost 100 percent yield of the desired dipeptide; higher water content accelerated the reaction reducing at the same time the yield of Ac-Tyr-Gly-NH2 due to the concurrent hydrolysis of the ester Ac-Tyr-OEt.No reaction was observed in the absence of base (triethylamine), wereas an excess of base only retarded the reaction.The enzyme is capable of catalyzing the peptide bond synthesis with N-acylamino acids or N-acyl peptides as acylating components, which may contain all types of L-amino acid residues (except Pro) in the P1 position.However, the peptide bond synthesis depends strongly on the amino component composition, particularly on the amino acid residue in the P'1 position.Only amides of glycine and of hydrophillic amino acids were acylated with Ac-Tyr-OEt; amides of hydrophobic amino acids enter the reaction only reluctantly or not at al.The presence of Leu or Phe in position P'2 and Leu in position P'3 has not so negative effect on acylation of the amino component as has in presence in the P'1 position.The choice of protecting groups for the α-carboxyl of the amino component is restricted only to amide and in some cases its undesired enzymatic removal was observed.Unprotected peptides seem to be suitable amino components.