3062-14-4

Usage

Uses

Used in Biochemistry Research:
H-ASP-LEU-OH is used as a research tool for studying the interactions and functions of amino acids in biological systems, particularly in the context of peptide synthesis and enzymatic reactions.
Used in Medicinal Chemistry:
H-ASP-LEU-OH is used as a building block in the design and synthesis of novel peptide-based drugs, leveraging its unique properties to target specific biological pathways or receptors.
Used in Pharmaceutical Development:
H-ASP-LEU-OH is used as a potential therapeutic agent for the treatment of various diseases and conditions, given its role in protein synthesis and muscle growth, as well as its potential to modulate specific biological processes.
Used in Drug Delivery Systems:
H-ASP-LEU-OH can be employed in the development of innovative drug delivery systems, where its peptide nature may facilitate targeted delivery and enhanced bioavailability of therapeutic agents.
Used in Nutritional Supplements:
H-ASP-LEU-OH may be incorporated into nutritional supplements to support protein synthesis, muscle growth, and overall health, capitalizing on the benefits of its constituent amino acids.

InChI:InChI=1/C10H18N2O5/c1-5(2)3-7(10(16)17)12-9(15)6(11)4-8(13)14/h5-7H,3-4,11H2,1-2H3,(H,12,15)(H,13,14)(H,16,17)

Upstream product

• 2462-35-3 L-leucine benzyl ester hydrochloride 
• 1738-69-8 L-Leucine benzyl ester 
• 119278-21-6 N-(O-benzyl-N-benzyloxycarbonyl-L-α-aspartyl)-L-leucine benzyl ester 

Relevant academic research and scientific papers

DPP4 INHIBITOR AND PHARMACEUTICAL APPLICATION THEREOF

The present invention provides a Dpp4 inhibitor which comprises a leucine derivative of the following formula (1) or a methionine derivative of the following formula (2): wherein each R1 and R3 represents a hydrogen atom (H) and an L-amino acid residue; R2 represents a hydroxyl group (OH), alkoxy group having 1 to 6 carbon atoms, amino group (NH2), alkylamino group having 1 to 6 carbon atoms, glycine residue, β-alanine residue, L-amino acid (except for proline, alanine and phenylalanine) residue or L-amino-acid amide (except for proline amide, alanine amide and phenylalanine amide) residue; and R4 represents a hydroxyl group (OH), alkoxy group having 1 to 6 carbon atoms, amino group (NH2), alkylamino group having 1 to 6 carbon atoms, glycine residue, β-alanine residue, L-amino acid (except for proline and alanine) residue or L-amino-acid amide (except for proline amide and alanine amide) residue. These derivatives also act as autophagy regulators.

Isolation and identification of urinary β-aspartyl dipeptides and their concentrations in human urine

β-Aspartyl-methionine, -aspartic acid and -glutamic acid and γ-glutamyl-threonine and -glycine were isolated and identified in human urine by means of ion-exchange chromatography, highvoltage paper electrophoresis, acid hydrolysis and determination of N-terminal amino acids of the isolated compounds, and comparison of their behaviors in paper electrophoresis and chromatography with those of the authentic compounds. The concentrations of acidic β-aspartyl dipeptides in human urine were determined using an amino acid analyzer. Their concentrations were as follows: β-aspartyl-glycine, male, 44.4±8.5, female, 61.4±18.9, child, 83.7±27.1; -alanine, male, 11.0±4.9, female, 20.7±12.0, child, 25.3±9.1; -glutamic acid, male, 10.0±3.7, female, 23.0±8.5, child, 20.4±7.5; -serine, male, 9.9±2.8, female, 13.6±3.8, child, 14.9±4.7; -aspartic acid, male, 4.3±1.0, female, 9.1±2.2, child, 18.4±6.5; -threonine, male, 3.9±0.9, female, 5.8±1.1, child, 13.2±4.9 μmol/g creatinine (mean ± S.D.). The order of the sum of their concentrations tended to be child>female>male. Patients receiving intravenous hyperalimentation also excreted acidic β-aspartyl dipeptides into urine in amounts similar to those in females and in a pattern similar to that observed in healthy persons. This finding indicates that urinary β-aspartyl dipeptides were probably of endogenous origin because oral nutrition was stringently excluded in these patients.