42384-22-5

Upstream product

• 58889-73-9 (S)-N-benzyloxycarbonyl-leucine ethyl ester 
• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 501-53-1 benzyl chloroformate 
• 51021-87-5 N-benzyloxycarbonyl-L-leucine methyl ester 
• 7803-57-8 hydrazine hydrate 
• 61-90-5 L-leucine 
• 2666-93-5 (S)-Leu-OMe 

Downstream Products

• 76863-45-1 (S)-benzyl (1-azido-4-methyl-1-oxopentan-2-yl)carbamate 
• 13588-95-9 L-leucyl-L-valine 
• 103238-78-4 Benzyloxycarbonyl-L-leucyl-L-valin-benzylester 
• 190660-78-7 (1S)-1-benzyloxycarbonylamino-3-methyl-1-(1,3,4-oxadiazol-2-on-5-yl)butane 
• 2873-36-1 cyclo(L-Pro-L-Leu) 
• 1246168-80-8 C₁₉H₂₈N₄O₅S 
• 1360470-89-8 C₂₂H₃₁N₃O₅S 
• 1356072-77-9 benzyl (1S)-1-isobutyl-2-{(2E/Z)-2-[(5-nitro-2-furyl)-methylene]hydrazine}-2-oxoethylcarbamate 
• 20806-85-3 N-[N-(N-benzyloxycarbonyl-L-leucyl)-glycyl]-glycine ethyl ester 
• 14297-22-4 N-[N-(N-benzyloxycarbonyl-L-leucyl)-glycyl]-glycine 
• 1187-50-4 L-Leu-Gly-Gly 

Relevant academic research and scientific papers

AMINOCARBAMOYL COMPOUNDS FOR THE TREATMENT OF VIRAL INFECTIONS

The present invention relates to compounds of formula (II) wherein R1-R5, X and L are as described herein, and pharmaceutically acceptable salts thereof, compositions including the compounds and methods of using the compounds, particularly in the treatment and prophylaxis of coronavirus infection.

Self-assembled organogels formed by L-leucine dihydrazide derivative

A new organogelator, benzyl (4-methyl-1-oxo-1-(2-hexadecanoylhydrazinyl) pentan-2-yl)carbamate (designated as Cbz-Leu-HdHz), was designed and synthesized, which could self-assemble in many organic solvents and form the thermally reversible physical supram

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).

A favorable, narrow, δh Hansen-parameter domain for gelation of low-molecular-weight amino acid derivatives

In recent years, the design of new low-molecular-weight gelators (LMWGs) has attracted considerable attention because of the interesting supramolecular architectures as well as industrial applications. In this context, the role of the organic solvent in d

A family of strong low-molecular-weight organogelators based on aminoacid derivatives

A new family of potent aminoacid-type organogelators obtained via an easy and unexpensive way is described. We demonstrated that structural variations onto the side chains of the aminoacid derivatives allowed modulations of the gelation properties. The or

Treatment of parasitic diseases by inhibition of cysteine proteases of the papain superfamily

The present invention relates to compounds and pharmaceutical compositions which inhibit proteases, such as cysteine proteases. In particular, the present invention relates to compounds and pharmaceutical compositions which inhibit cysteine proteases of the papain superfamily. The compounds and pharmaceutical compositions of the present invention are useful for treating diseases, particularly parasitic diseases, which are mediated by such proteases. In particular, the present invention relates to a method of treating malaria by inhibiting the cysteine protease falcipain.

New system for peptide synthesis using N-acylpyrazoles

New system of peptide synthesis was described. The extension of one amino acid unit on the peptide chain was constituted from only 2 reaction steps, the conversion from esters to the corresponding N-acylpyrazoles and the subsequent aminolysis with amino esters. This new system was distinctive from the conventional peptide synthesis, which was consisted of 3 steps of the deprotection, the activation and the condensation. Moreover, the key intermediate N-acylpyrazoles exhibited the excellent properties of high sensitivity and separability for the chiral column on HPLC using the UV detector.

Structure-based design of non-peptide, carbohydrazide-based cathepsin K inhibitors

Using binding models which were based on the X-ray crystal structure of an amino acid-based active site-spanning inhibitor complexed with cathepsin K, Cbz-leucine mimics have been developed, leading ultimately to the design of a potent cathepsin K inhibitor free of amino acid components. These mimics, which consist of α-substituted biphenylacetyl groups in place of Cbz-leucine moieties, effectively mimic all aspects of the Cbz-leucine moieties which are important for inhibitor binding. The predicted directions of binding for the inhibitors were confirmed by mass spectral analysis of their complexes with cathepsin K, which gave results consistent with acylation of the enzyme and loss of the acylhydrazine portion of the inhibitor which binds on the S' side of the active site. The binding models were found to be very predictive of relative inhibitor potency as well as direction of inhibitor binding. These results strengthen the validity of a strategy involving iterative cycles of structure-based design and inhibitor synthesis and evaluation for the discovery of non-peptide inhibitors. Copyright (C) 1999 Elsevier Science Ltd.

PROTEASE INHIBITORS

Disclosed herein is a compound of the formula STR1 known as 2-[N-(N-benzyloxycarbonyl-L-leucinyl)]-2'-[N'-[4-(N,N-dimethylaminomethyl) benzyloxy]carbonyl-L-leucinyl]carbohydrazide; and pharmaceutically acceptable salts, hydrates and solvates thereof.

Structure-based design of cathepsin K inhibitors containing a benzyloxy- substituted benzoyl peptidomimetic

Peptidomimetic cathepsin K inhibitors have been designed using binding models which were based on the X-ray crystal structure of an amino acid- based, active site-spanning inhibitor complexed with cathepsin K. These inhibitors, which contain a benzyloxybenzoyl group in place of a Cbz-leucine moiety, maintained good inhibitory potency relative to the amino acid-based inhibitor, and the binding models were found to be very predictive of relative inhibitor potency. The binding mode of one of the inhibitors was confirmed by X-ray crystallography, and the crystallographically determined structure is in close qualitative agreement with the initial binding model. These results strengthen the validity of a strategy involving iterative cycles of structure-based design, inhibitor synthesis and evaluation, and crystallographic structure determination for the discovery of peptidomimetic inhibitors.