6278-97-3

Usage

Uses

Used in Pharmaceutical Development:
H-DL-LEU-NHNH2 is used as a key component in the development of pharmaceuticals for its ability to contribute to the synthesis of bioactive peptides and other medicinal compounds. Its unique structure allows it to be a valuable building block in the creation of new drugs with specific therapeutic properties.
Used in Peptide Synthesis:
In the field of peptide synthesis, H-DL-LEU-NHNH2 is utilized as a starting material or intermediate in the assembly of larger peptide chains. Its presence in the synthesis process can influence the properties and functions of the resulting peptides, making it an important factor in the design of peptide-based therapeutics.
Used in Research and Laboratory Settings:
H-DL-LEU-NHNH2 is used as a research tool for studying the structure and function of proteins and peptides. Its role in these studies aids in understanding the fundamental biology of these macromolecules and can lead to insights that inform the development of new treatments and therapies.
Used in Drug Design and Discovery:
In the process of drug design and discovery, H-DL-LEU-NHNH2 is employed as a component in the design of new drugs. Its unique properties can be leveraged to create molecules with specific binding affinities or activities, contributing to the advancement of pharmaceutical research.
Used in Peptide-based Materials Production:
H-DL-LEU-NHNH2 is also used in the production of peptide-based materials, where its incorporation can impart specific characteristics to the material, such as enhanced stability, biocompatibility, or targeted biological activity. This makes it a valuable component in the development of materials for various applications, including medical devices and drug delivery systems.

Upstream product

• 6322-53-8 leucine methyl ester hydrochloride 
• 2899-43-6 DL-leucine ethyl ester 
• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 7803-57-8 hydrazine hydrate 
• 61-90-5 L-leucine 
• 1115-39-5 N-trifluoroacetyl methyl ester of (S)-leucine 
• 2666-93-5 (S)-Leu-OMe 
• 2743-60-4 L-Leucine ethyl ester 

Downstream Products

• 1165943-77-0 N'-[(2E/Z)-4-nitrobenzylidene]-(2S)-amino-4-methylpentanehydrazide 
• 1587732-44-2 (S,E)-2-amino-4-methyl-N'-(3-(trifluoromethyl)benzylidene)pentanehydrazide 
• 1587732-52-2 (S,Z)-2-amino-4-methyl-N'-(3-(trifluoromethyl)benzylidene)pentanehydrazide 
• 2021-47-8 (2S)-2-amino-4-methylpentanehydrazide 
• 61-90-5 L-leucine 

Relevant academic research and scientific papers

Chiral arylideneaminoimidazolidin-4-ones: Green synthesis and isomerisation mechanism in solution

A green and eco-friendly synthetic approach of pure 2,5-disubstituted 3-arylideneaminoimidazolidin-4-ones is developed using water as the solvent. These new chiral arylideneaminoimidazolidin-4-one derivatives were obtained diastereoselectively in high ove

Fragment Linking and Optimization of Inhibitors of the Aspartic Protease Endothiapepsin: Fragment-Based Drug Design Facilitated by Dynamic Combinatorial Chemistry

Fragment-based drug design (FBDD) affords active compounds for biological targets. While there are numerous reports on FBDD by fragment growing/optimization, fragment linking has rarely been reported. Dynamic combinatorial chemistry (DCC) has become a powerful hit-identification strategy for biological targets. We report the synergistic combination of fragment linking and DCC to identify inhibitors of the aspartic protease endothiapepsin. Based on X-ray crystal structures of endothiapepsin in complex with fragments, we designed a library of bis-acylhydrazones and used DCC to identify potent inhibitors. The most potent inhibitor exhibits an IC50value of 54 nm, which represents a 240-fold improvement in potency compared to the parent hits. Subsequent X-ray crystallography validated the predicted binding mode, thus demonstrating the efficiency of the combination of fragment linking and DCC as a hit-identification strategy. This approach could be applied to a range of biological targets, and holds the potential to facilitate hit-to-lead optimization.

Structure-based design of inhibitors of the aspartic protease endothiapepsin by exploiting dynamic combinatorial chemistry

Structure-based design (SBD) can be used for the design and/or optimization of new inhibitors for a biological target. Whereas de novo SBD is rarely used, most reports on SBD are dealing with the optimization of an initial hit. Dynamic combinatorial chemistry (DCC) has emerged as a powerful strategy to identify bioactive ligands given that it enables the target to direct the synthesis of its strongest binder. We have designed a library of potential inhibitors (acylhydrazones) generated from five aldehydes and five hydrazides and used DCC to identify the best binder(s). After addition of the aspartic protease endothiapepsin, we characterized the protein-bound library member(s) by saturation-transfer difference NMR spectroscopy. Cocrystallization experiments validated the predicted binding mode of the two most potent inhibitors, thus demonstrating that the combination of de novo SBD and DCC constitutes an efficient starting point for hit identification and optimization. The dynamic duo: The combination of de novo structure-based design and dynamic combinatorial chemistry has been applied to the identification of novel acylhydrazone-based inhibitors for the aspartic protease endothiapepsin. 1H-STD-NMR spectroscopy has been used to identify the binders from the dynamic combinatorial libraries. Proposed binding modes of the most potent inhibitors have been confirmed by X-ray crystallography.

In situ deprotection and incorporation of unnatural amino acids during cell-free protein synthesis

The S30 extract from E. coli BL21 Star (DE3) used for cell-free protein synthesis removes a wide range of α-amino acid protecting groups by cleaving α-carboxyl hydrazides; methyl, benzyl, tert-butyl, and adamantyl esters; tert-butyl and adamantyl carboxamides; α-amino form-, acet-, trifluoroacet-, and benzamides and sidechain hydrazides and esters. The free amino acids are produced and incorporated into a protein under standard conditions. This approach allows the deprotection of amino acids to be carried out in situ to avoid separate processing steps. The advantages of this approach are demonstrated by the efficient incorporation of the chemically intractable (S)-4-fluoroleucine, (S)-4,5- dehydroleucine, and (2S,3R)-4-chlorovaline into a protein through the direct use of their respective precursors, namely, (S)-4-fluoroleucine hydrazide, (S)-4,5-dehydroleucine hydrazide, and (2S,3R)-4-chlorovaline methyl ester. These results also show that the fluoroand dehydroleucine and the chlorovaline are incorporated into a protein by the normal biosynthetic machinery as substitutes for leucine and isoleucine, respectively. Copyright

Synthesis and Antitubercular Activity of Novel Amino Acid Derivatives

In this work, 17 new N-acylhydrazone derivatives of amino acids have been evaluated for their in vitro antibacterial activity against Mycobacterium tuberculosis H37Rv. The compounds 8b, 8e, 8f, 9a-d, and 10c exhibited an important minimum inhibitory concentration activity between 12.5 and 50μg/mL, which can be compared with that of the tuberculostatic drug d-cycloserine (20μg/mL). In this work 17 new N-acylhydrazone derivatives of amino acids have been evaluated for their in vitro antibacterial activity against Mycobacterium tuberculosis H37Rv. Eight compounds were non-cytotoxic and exhibited an important MIC activity between 12.5 and 50μg/mL, which can be compared with that of the tuberculostatic drug d-cycloserine (20μg/mL).

Sandwich structure of a ruthenium porphyrin and an amino acid hydrazide for probing molecular chirality by circular dichroism

Owing to the strong Lewis acidity of ruthenium porphyrins, a commercial carbonyl ruthenium porphyrin and an amino acid hydrazide can assemble into a sandwich structure. The nature of such a structure is diagnostic of the absolute configuration of the amino acid by circular dichroism.