35436-83-0

Basic information

• Product Name: H-DL-LEU-DL-VAL-OH H2O
• Synonyms: D-Leu-D-Val-OH/D-Leu-L-Val-OH/L-Leu-D-Val-OH/L-Leu-L-Val-OH,(1:1:1:1);2-(2-Amino-4-methylpentanamido);DL-LEUCYL-DL-VALINE;DL-LEUCYL-DL-VALINE MONOHYDRATE;H-DL-LEU-DL-VAL-OH;H-DL-LEU-DL-VAL-OH H2O;Leucylvaline
• CAS NO: 35436-83-0
• Molecular Formula: C₁₁H₂₂N₂O₃
• Molecular Weight: 230.31
• Product Categories: Peptide Synthesis;Biochemistry;Oligopeptides
• Mol File: 35436-83-0.mol

Chemical Properties

• Boiling Point: 421.9oC at 760 mmHg
• Flash Point: 209oC
• Appearance: /
• Density: 1.066g/cm3
• Vapor Pressure: 2.66E-08mmHg at 25°C
• Refractive Index: 1.482
• PKA: 3.18±0.10(Predicted)
• CAS DataBase Reference: H-DL-LEU-DL-VAL-OH H2O(CAS DataBase Reference)
• NIST Chemistry Reference: H-DL-LEU-DL-VAL-OH H2O(35436-83-0)
• EPA Substance Registry System: H-DL-LEU-DL-VAL-OH H2O(35436-83-0)

Safety Data

• Hazardous Substances Data: 35436-83-0(Hazardous Substances Data)

Usage

Uses

Used in Nutritional Supplements:
H-DL-LEU-DL-VAL-OH H2O is used as a nutritional supplement to support muscle health and enhance protein synthesis. The presence of DL-leucine and DL-valine, both essential amino acids, makes this compound a valuable addition to dietary supplements designed to promote muscle repair and growth.
Used in Sports Nutrition:
In the sports nutrition industry, H-DL-LEU-DL-VAL-OH H2O is used as a performance enhancer to improve muscle metabolism and energy production. Athletes and fitness enthusiasts can benefit from the compound's ability to support muscle function and recovery during intense physical activities.
Used in Pharmaceutical Formulations:
H-DL-LEU-DL-VAL-OH H2O is utilized in pharmaceutical formulations for its potential therapeutic effects on muscle-related conditions. H-DL-LEU-DL-VAL-OH H2O's role in muscle repair and metabolism may offer benefits in the treatment of muscle wasting diseases or conditions that impair muscle function.
Used in Cosmetics and Skincare:
In the cosmetics and skincare industry, H-DL-LEU-DL-VAL-OH H2O is used as a hydrating agent to improve skin moisture and elasticity. H-DL-LEU-DL-VAL-OH H2O's ability to bind with water may contribute to its effectiveness in maintaining skin hydration and promoting a healthy skin barrier.
Used in Food and Beverage Industry:
H-DL-LEU-DL-VAL-OH H2O is employed in the food and beverage industry as a functional ingredient to enhance the nutritional profile of products. H-DL-LEU-DL-VAL-OH H2O's muscle health benefits can be incorporated into sports drinks, energy bars, or other health-focused food products to cater to consumers seeking muscle support and recovery.

InChI:InChI=1/C11H22N2O3/c1-6(2)5-8(12)10(14)13-9(7(3)4)11(15)16/h6-9H,5,12H2,1-4H3,(H,13,14)(H,15,16)

Upstream product

• 7801-70-9 Z-Leu-Val 
• 72-18-4 L-valine 
• 3190-70-3 L-leucine N-carboxyanhydride 
• 56374-31-3 N-(2-bromo-4-methyl-valeryl)-valine 
• 7664-41-7 ammonia 
• 76863-45-1 (S)-benzyl (1-azido-4-methyl-1-oxopentan-2-yl)carbamate 
• 4070-48-8 L-Valine methyl ester 
• 16652-76-9 L-valine benzyl ester p-toluenesulfonate salt 
• 84111-39-7 L-leucyl-L-valine benzyl ester 
• 4703-53-1 N-benzyloxycarbonyl-L-leucine hydrazide 
• 17645-49-7 L-valine benzyl ester benzenesulfonate 

Downstream Products

• 5625-50-3 cyclo-(Leu-Val) 
• 1217336-50-9 C₄₉H₇₁N₇O₁₂S 

Relevant articles and documents

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.

Urethane-protected amino acid-N-carboxyanhydrides

Urethane-protected NCAs and MTAs are prepared by reacting an NCA or NTA with a haloformate in an inert diluent, under anhydrous conditions and in the presence of a tertiary nitrogen-containing base having an atom or functional group sufficiently electron rich and positioned relative to the nitrogen of said base so as to render said atom or group capable of complexing with the H--N group of said N-carboxyanhydride or N-thiocarboxyanhydride but able to generate N-carboxyanhydride or N-thiocarboxyanhydride anionic complexes capable of reacting with the haloformate.

Urethane-protected amino acid-N-carboxyanhydrides

The invention relates to urethane-protected amino acid-N-carboxyanhydride and N-thiocarboxyanhydride compounds which are useful in peptide, polypeptide and protein synthesis. Disclosed herein is the preparation and use of these novel compounds.

The Steric Hindrance of the Stepwise Reaction of N-Carboxy α-Amino Acid Anhydride with the α-Amino Acid Ester

The mechanisms of the reactions of 4-alkyloxazolidinediones (1) (N-carboxy α-amino acid anhydrides(NCAs)) with α-amino acid benzyl ester p-toluenesulfonates (2) were investigated in acetonitrile containing triethylamine at low and room temperatures.Two types of reactions were observed: (1) the polymerization of NCAs was initiated with a small amount of 2 to produce polypeptides (6), and (2) the dipeptide benzyl esters (4) were produced by the stepwise reaction of NCAs with the esters.Both the polymerization and the dipeptide formation (1+2) seemed to be initiated by the nucleophilic attack of the amino group of the ester on the C-5 carbon of NCAs.The polymerization proceeded when the side chains of the amino acid esters (R2) were more bulky than those of the NCAs (R1).On the contrary, dipeptide esters were produced when the side chains of the NCAs (R1) were more bulky than those of the esters (R2).