13588-95-9

Usage

Uses

Used in Pharmaceutical Industry:
H-LEU-VAL-OH is used as a therapeutic agent for inhibiting movement-induced muscle damage and muscle defective conditions. Its dipeptide structure allows for better absorption and utilization by the body, making it an effective treatment option for muscle-related issues.
Used in Sports Nutrition Industry:
H-LEU-VAL-OH is used as a performance enhancer and muscle recovery aid for athletes. Its ability to inhibit muscle damage and improve muscle function makes it a valuable addition to sports supplements and nutrition programs.
Used in Cosmetics Industry:
H-LEU-VAL-OH is used as an active ingredient in anti-aging and skin care products. Its dipeptide composition can help improve skin elasticity, reduce the appearance of fine lines and wrinkles, and promote overall skin health.
Used in Research and Development:
H-LEU-VAL-OH is used as a research compound for studying the effects of dipeptides on muscle function, protein synthesis, and other biological processes. Its unique properties make it an important tool in the development of new drugs and therapies for various conditions.

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)/t8-,9-/m0/s1

Upstream product

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

Downstream Products

• 1217336-50-9 C₄₉H₇₁N₇O₁₂S 

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.

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).