225386-32-3

Usage

Uses

Used in Antimicrobial Applications:
Z-N-ME-L-2-AMINOHEXANOIC ACID is used as an antimicrobial agent for its effectiveness against drug-resistant bacteria. Its unique structure allows it to target and inhibit the growth of various pathogenic bacteria, offering a promising solution to the growing problem of antibiotic resistance.
Used in Cancer Therapy:
In the field of oncology, Z-N-ME-L-2-AMINOHEXANOIC ACID is used as a potential therapeutic agent for its ability to inhibit enzymes that play a role in cancer progression. By targeting these enzymes, it may help to slow down or prevent the growth and spread of cancer cells, offering a new avenue for cancer treatment.
Used in Neurodegenerative Disease Treatment:
Z-N-ME-L-2-AMINOHEXANOIC ACID is utilized in the treatment of neurodegenerative diseases as a neuroprotective agent. Its capacity to protect neurons from oxidative stress and inflammation makes it a valuable candidate for the development of therapies aimed at slowing down or halting the progression of these debilitating conditions.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, Z-N-ME-L-2-AMINOHEXANOIC ACID is used as a building block for the synthesis of various drugs and drug candidates. Its unique properties and potential applications make it a valuable compound for the development of new therapeutic agents across different medical fields.
Used in Cosmetics Industry:
Z-N-ME-L-2-AMINOHEXANOIC ACID may also find applications in the cosmetics industry, where it could be used as an active ingredient in skincare products. Its antimicrobial and anti-inflammatory properties could contribute to the development of products aimed at improving skin health and combating skin conditions.
Used in Agricultural Industry:
In agriculture, Z-N-ME-L-2-AMINOHEXANOIC ACID could be employed as a biopesticide or a component in the development of pest-resistant crops. Its antimicrobial properties may help to protect plants from bacterial infections, contributing to increased crop yields and reduced reliance on chemical pesticides.

Upstream product

• 39608-30-5 N-benzyloxycarbonyl-L-norleucine 
• 74-88-4 methyl iodide 
• 225386-50-5 phenylmethyl (4S)-4-butyl-5-oxo-1,3-oxazolidine-3-carboxylate 

Downstream Products

• 264887-55-0 N-benzyloxycarbonyl-N-methyl-L-norleucinyl-L-norleucine methyl ester 
• 264887-70-9 N-benzyloxycarbonyl-N-methyl-L-norleucyl-L-norleucine 
• 922705-69-9 phenylmethyl [(1S)-1-(diazoacetyl)pentyl]methylcarbamate 
• 1445444-34-7 (3S)-N-benzyloxycarbonyl-3-aminomethyl-1-nitroheptane 
• 1445443-98-0 (3S)-N-benzyloxycarbonyl-3-aminomethyl-2-hydroxy-1-nitroheptane 
• 1445443-38-8 (S)-benzyl (1-hydroxyhexan-2-yl)(methyl)carbamate 
• 264887-71-0 N-benzyloxycarbonyl-N-methyl-L-norleucyl-L-norleucine methylamide 
• 922705-48-4 (3S)-3-(methyl{[(phenylmethyl)oxy]carbonyl}amino)heptanoic acid 

Relevant academic research and scientific papers

Effective methods for the synthesis of N-methyl β-amino acids from all twenty common α-amino acids using 1,3-oxazolidin-5-ones and 1,3-oxazinan-6-ones

N-Methyl β-amino acids are generally required for application in the synthesis of potentially bioactive modified peptides and other oligomers. Previous work highlighted the reductive cleavage of 1,3-oxazolidin-5-ones to synthesise N-methyl α-amino acids. Starting from α-amino acids, two approaches were used to prepare the corresponding N-methyl β-amino acids. First, α-amino acids were converted to N-methyl α-amino acids by the so-called '1,3-oxazolidin-5-one strategy', and these were then homologated by the Arndt-Eistert procedure to afford N-protected N-methyl β-amino acids derived from the 20 common α-amino acids. These compounds were prepared in yields of 23-57% (relative to N-methyl α-amino acid). In a second approach, twelve N-protected α-amino acids could be directly homologated by the Arndt-Eistert procedure, and the resulting β-amino acids were converted to the 1,3-oxazinan-6-ones in 30-45% yield. Finally, reductive cleavage afforded the desired N-methyl β-amino acids in 41-63% yield. One sterically congested β-amino acid, 3-methyl-3-aminobutanoic acid, did give a high yield (95%) of the 1,3-oxazinan-6-one (65), and subsequent reductive cleavage gave the corresponding AIBN-derived N-methyl β-amino acid 61 in 71% yield (Scheme 2). Thus, our protocols allow the ready preparation of all N-methyl β-amino acids derived from the 20 proteinogenic α-amino acids.

Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: A strategy for the design of peptidase inhibitors

The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase which has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10). It cleaves the neurotransmitter CCK-8 sulfate at the Met-Gly bond to give Asp-Tyr(SO3H)-Met-OH + Gly-Trp-Met-Asp-Phe-NH2. In seeking a reversible inhibitor of this peptidase, the enzymatic binding subsites were characterized using a fluorimetric assay based on the hydrolysis of the artificial substrate Ala-Ala-Phe-amidomethylcoumarin. A series of di- and tripeptides having various alkyl or aryl side chains was studied to determine the accessible volume for binding and to probe the potential for hydrophobic interactions. From this initial study the tripeptides Ile-Pro-Ile-OH (K(i) = 1 μM) and Ala-Pro-Ala-OH (K(i) = 3 μM) and dipeptide amide Val-Nvl-NHBu (K(i) = 3 μM) emerged as leads. Comparison of these structures led to the synthesis of Val-Pro-NHBu (K(i) = 0.57 μM) which served for later optimization in the design of butabindide, a potent reversible competitive and selective inhibitor of the CCK-8-inactivating peptidase. The strategy for this work is explicitly described since it illustrates a possible general approach for peptidase inhibitor design.