15893-47-7

Usage

Uses

Used in Pharmaceutical Research:
H-D-LEU-NH2 is used as a research compound for understanding the role of leucine in protein structure and function, which is essential for the development of therapeutic agents targeting muscle-related conditions and protein synthesis disorders.
Used in Protein Synthesis Studies:
In the field of biochemistry, H-D-LEU-NH2 is employed as a model compound to study the mechanisms of protein synthesis, offering insights into the processes that govern muscle repair and growth.
Used in Muscle Repair and Growth Applications:
H-D-LEU-NH2 is utilized as a nutritional supplement in the sports and fitness industry to support muscle repair and growth, capitalizing on its role in protein synthesis and muscle maintenance.
Used in Drug Development:
In the pharmaceutical industry, H-D-LEU-NH2 is used as a key component in the development of drugs aimed at treating conditions related to muscle wasting and protein synthesis deficiencies, leveraging its inherent properties to enhance muscle health and function.

Upstream product

• 13079-20-4 2-Amino-4-methyl-pentanoic acid amide 
• 220184-57-6 (R)-2-(2-Methoxy-6-methyl-phenylamino)-4-methyl-pentanoic acid amide 
• 70533-96-9 N-tert-butoxycarbonyl-(L)-leucinamide 
• 61-90-5 L-leucine 
• 4801-79-0 N-benzyloxycarbonyl-L-leucinamide 
• 106827-71-8 Trt-L-Hse(Trt)-L-Leu-NH₂ 
• 60117-24-0 H-Tyr-Gly-Gly-Phe-Leu-NH₂ 
• 869-19-2 Glycyl-L-leucine 
• 7664-41-7 ammonia 
• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 139551-97-6 (S)-(9H-fluoren-9-yl)methyl (1-Amino-4-methyl-1-oxo-pentan-2-yl)carbamate 
• 35661-60-0 Fmoc-Leu-OH 
• 2666-93-5 (S)-Leu-OMe 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 

Downstream Products

• 92489-58-2 N-CBZ-L-Tyr-D-LeuNH₂ 
• 132402-95-0 Mal-Tyr-D-Leu-NH₂ 
• 1161-13-3 N-Cbz-L-Phe 
• 13171-94-3 Z-Phe(D)LeuNH₂ 
• 56672-76-5 1-hippuroyl-L-proline 
• 2018-66-8 Z-Leu-OH 
• 28862-79-5 Z-D-Leu-OH 
• 279255-90-2 tert-butyl 5-(hydroxymethyl)-1H-indole-1-carboxylate 
• 879887-21-5 2R-(1-t-butyloxycarbonylindol-5-ylmethylamino)-4-methyl-pentanamide 
• 879887-65-7 2R-bis-(1-t-butyloxycarbonylindol-5-ylmethyl)amino-4-methylpentanamide 
• 70497-43-7 Carbobenzoxy-S-benzyl-cysteinyl-leucinamid-(L,L) 
• 17193-48-5 Z-(β-O-Bz-Asp)-Leu-NH2 
• 59937-71-2 (S)-4-Methyl-2-(2-nitro-phenylsulfanylamino)-pentanoic acid amide 

Relevant academic research and scientific papers

Mapping the s1 and s1’ subsites of cysteine proteases with new dipeptidyl nitrile inhibitors as trypanocidal agents

The cysteine protease cruzipain is considered to be a validated target for therapeutic intervention in the treatment of Chagas disease. A series of 26 new compounds were designed, synthesized, and tested against the recombinant cruzain (Cz) to map its S1/S1′ subsites. The same series was evaluated on a panel of four human cysteine proteases (CatB, CatK, CatL, CatS) and Leishmania mexicana CPB, which is a potential target for the treatment of cutaneous leishmaniasis. The synthesized compounds are dipeptidyl nitriles designed based on the most promising combinations of different moieties in P1 (ten), P2 (six), and P3 (four different building blocks). Eight compounds exhibited a Ki smaller than 20.0 nM for Cz, whereas three compounds met these criteria for LmCPB. Three inhibitors had an EC50 value of ca. 4.0 μM, thus being equipotent to benznidazole according to the antitrypanosomal effects. Our mapping approach and the respective structure-activity relationships provide insights into the specific ligand-target interactions for therapeutically relevant cysteine proteases.

Bianthryl-based organocatalysts for the asymmetric Henry reaction of fluoroketones

We have developed a catalytic system based on bianthrylbis(thiourea) for the asymmetric Henry reaction of fluoroketones and nitroalkanes that resulted from the screening of a library containing 31 chiral non-racemic organocatalysts. The corresponding adducts were isolated in up to 6 times shorter reaction time in comparison with the previously published organocatalysts. High levels of stereocontrol have been generally observed, with measured product enantiomeric excesses up to 97% and diastereomeric ratio 3:2 (anti/syn). The above-mentioned catalysts have been successfully applied to the total asymmetric synthesis of CF3-tethered (S)-halostachines, which has proved that this method constitutes an easy entry to similar enantiopure compounds.

HEMIAMINAL-TAG FOR PROTEIN LABELING AND PURIFICATION

The invention pertains to the synthesis, isolation, and characterization of hemiaminal for selective labeling of peptides, proteins, antibodies, and organic fragments with -C(=0) CH2NH2 and derivatives with -CH2NH2 group over -C(=0) CHRNH2 group (where R≠H). The invention also pertains to the method of single-site immobilization of proteins through N-terminus Gly on solid phase. The invention includes late-stage tagging of N-terminus Gly with an affinity tag, 19F NMR probe, and a fluorophore and a method for metal-free protein purification and isolation of analytically pure proteins.

3, 5-disubstituted hydantoin compound as well as preparation method and application thereof

The invention provides a 3, 5-disubstituted hydantoin compound as well as a preparation method and an application thereof. The structure of the compound is shown in formula I in the description. The application of the 3, 5-disubstituted hydantoin compound shown in the formula I or solvates, hydrates or salts of the compound in preparation of medicines for treating Alzheimer's disease, vascular dementia and other dementia diseases with memory impairment also belongs to the protection scope. Animal experiments prove that the compound has the effect of saving memory of animal models, has high safety, does not have mutagenicity, can stay in blood for several hours after oral administration and intravenous injection, and can enter the brain.

Synthetic method for chiral alpha-aminoamide compounds

The invention provides a synthetic method for chiral alpha-aminoamide compounds, belongs to the technical field of organic synthetic methodology, and concretely relates to a synthetic method for chiral alpha-aminoamide compounds, wherein the method has a simple process, low costs and good economy. The method comprises the following steps: 1, performing ammonolysis: adding substituted chiral alpha-aminocarboxylate hydrochloride into concentrated ammonia water, performing stirring for 4-12h under a room temperature, wherein each 1mmol substituted chiral alpha-aminocarboxylate hydrochloride is corresponding to 2-8mL the concentrated ammonia water; 2, after a reaction is finished, performing distillation for removing ammonia water after the reaction to obtain crude products chiral alpha-aminoamide compounds; and 3, performing filtration on the obtained crude products chiral alpha-aminoamide compounds by adopting a manner of adding a solvent or performing purification on the obtained crude products chiral alpha-aminoamide compounds through a manner of column chromatography which uses ammonia water as a mobile phase to obtain the products chiral alpha-aminoamide compounds. Compared with the prior art, a large number of an ammonia gas for ammonolysis is not needed in the method, the process and post-treatment are simple, costs are low and reaction time is short.

SYNTHESIS OF ARYL CYCLOHEXANE CARBOXAMIDE DERIVATIVES USEFUL AS SENSATES IN CONSUMER PRODUCTS

Synthesis methods to produce a series of carboxamides built off of an (S)-2-amino acid backbone or an (R)-2-amino acid backbone, depending upon the desired diastereomer of the end product.

AMIDE COMPOUNDS, METHODS FOR PREPARATION, AND USE THEREOF AS AGENTS FOR THE TREATMENT AND PREVENTION OF DISEASES CAUSED BY RNA- AND/OR DNA-CONTAINING VIRUSES, AND CONCOMITANT DISEASES

The present invention relates to medicine and includes a method for preventing and treating diseases caused by RNA- and DNA-containing viruses, and concomitant diseases, wherein the method comprises the use of an effective amount of compounds of general formula I or pharmaceutically acceptable salts thereof. The invention also relates to methods for preparing said compounds, pharmaceutical compositions for the prevention or treatment of diseases caused by RNA- and DNA-containing viruses, said compositions comprising an effective amount of a compound of formula I or a pharmaceutically acceptable salt thereof. The invention addresses the object of providing a novel agent effective in the treatment of diseases caused by an RNA-containing virus belonging to the Enterovirus, Metapneumovirus, Pneumovirus, Respirovirus, or Alfa-coronavirus genus, and/or by a DNA-containing virus belonging to the Adenoviridae and/or Herpesviridae family, and in the prevention and treatment of asthma exacerbation, chronic obstructive pulmonary disease, mucoviscidosis, conjunctivitis, gastroenteritis, hepatitis, myocarditis; in the prevention and treatment of rhinorrhea, acute and infectious rhinitis, pharyngitis, nasopharyngitis, tonsillitis, laryngitis, laryngotracheitis, laryngotracheobronchitis, bronchitis, bronchiolitis, pneumonia, or airway obstructive syndrome.

Gastrin releasing peptide receptor-directed radioligands based on a bombesin antagonist: Synthesis, 111in-labeling, and preclinical profile

Novel bombesin (BBN) antagonists were synthesized by coupling the chelator 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid (DOTA) to H-d-Phe-Gln-Trp-Ala-Val-Gly-His-Sta-Leu-NH2 (JMV594) through linkers of increasing number of (βAla)x residues (x = 1-3). Labeling with 111In afforded the respective radiotracers in high purity and high specific activity. Bioconjugate affinity for the gastrin releasing peptide receptor (GRPR) as determined against [125I-Tyr4]BBN was high (IC50 values in the lower nanomolar range). Radioligands poorly internalized in PC-3 cells at 37 C. Radiopeptides remained >60% intact 5 min after entering the bloodstream of healthy mice. After injection in SCID mice bearing human PC-3 xenografts all analogues showed high tumor uptake and rapid background clearance via the kidneys into urine. Interestingly, pancreatic uptake, albeit GRPR-specific, declined rapidly with time. 111In-DOTA- (βAla)2-JMV594 achieved the highest tumor values among the group (17.0 ± 2.8%ID/g vs. 8-10%ID/g, respectively, at 4 h pi) indicating that the (βAla)2-linker favors in vivo interaction of radiopeptides with the GRPR.

Development and evaluation of novel phosphotyrosine mimetic inhibitors targeting the Src homology 2 domain of signaling lymphocytic activation molecule (SLAM) associated protein

Specific interactions between Src homology 2 (SH2) domain-containing proteins and the phosphotyrosine-containing counterparts play significant role in cellular protein tyrosine kinase (PTK) signaling pathways. The SH2 domain inhibitors could potentially serve as drug candidates in treating human diseases. Here we have incorporated a novel phosphotyrosine mimetic, which is an unusual amino acid carrying a cyclosaligenyl (cycloSal) phosphodiester moiety, into dipeptides to investigate the inhibitory effect on SH2 domain-containing proteins. A plate-based assay was also established to screen for inhibitors that disrupt the interaction between a phosphopeptide of SLAM (signaling lymphocytic activation molecule) and its interacting protein SAP (SLAM-associated protein). We identified a number of inhibitors with IC50 values in the range of 17-35 μM, implying that the cycloSal phosphodiester-carrying amino acid could mimic the phosphotyrosyl residue. Our results also raise the possibility of integrating the newly developed phosphotyrosine mimetic moiety into inhibitors designed for other SH2 domain-containing proteins.