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L-Leu-D-Val-OH is a dipeptide composed of the essential amino acid L-leucine and the non-proteinogenic amino acid D-valine. L-leucine plays a crucial role in protein synthesis and muscle growth, while D-valine possesses antiproliferative and neuroprotective properties. As a synthetic compound, L-Leu-D-Val-OH holds potential for applications in the pharmaceutical and biotechnology sectors, particularly in the development of innovative drugs and therapeutic agents. Its distinctive amino acid composition and structural features provide a foundation for further research and exploration in chemical biology and medicinal chemistry.

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  • 17665-00-8 Structure
  • Basic information

    1. Product Name: L-Leu-D-Val-OH
    2. Synonyms: N-L-Leucyl-D-valine;L-Leu-D-Val-OH
    3. CAS NO:17665-00-8
    4. Molecular Formula: C11H22N2O3
    5. Molecular Weight: 230.3
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 17665-00-8.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: N/A
    4. Appearance: /
    5. Density: N/A
    6. Refractive Index: N/A
    7. Storage Temp.: N/A
    8. Solubility: N/A
    9. CAS DataBase Reference: L-Leu-D-Val-OH(CAS DataBase Reference)
    10. NIST Chemistry Reference: L-Leu-D-Val-OH(17665-00-8)
    11. EPA Substance Registry System: L-Leu-D-Val-OH(17665-00-8)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 17665-00-8(Hazardous Substances Data)

17665-00-8 Usage

Uses

Used in Pharmaceutical Industry:
L-Leu-D-Val-OH is used as a building block for the development of new drugs and therapeutic agents due to its unique combination of amino acids and potential biological activities.
Used in Biotechnology Industry:
L-Leu-D-Val-OH is used as a component in the design of novel biotechnological applications, leveraging its structural properties and the functional attributes of its constituent amino acids for various purposes, such as enhancing protein synthesis or providing neuroprotection.
Used in Chemical Biology Research:
L-Leu-D-Val-OH is used as a subject of study in chemical biology to explore its interactions with biological systems and to understand its potential role in modulating biological processes, which could lead to the discovery of new therapeutic targets or mechanisms.
Used in Medicinal Chemistry:
L-Leu-D-Val-OH is utilized in medicinal chemistry for the synthesis of complex molecules and the investigation of its structure-activity relationships, which may contribute to the advancement of drug discovery and the optimization of pharmaceutical compounds.

Check Digit Verification of cas no

The CAS Registry Mumber 17665-00-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,7,6,6 and 5 respectively; the second part has 2 digits, 0 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 17665-00:
(7*1)+(6*7)+(5*6)+(4*6)+(3*5)+(2*0)+(1*0)=118
118 % 10 = 8
So 17665-00-8 is a valid CAS Registry Number.

17665-00-8Downstream Products

17665-00-8Relevant articles and documents

DPP4 INHIBITOR AND PHARMACEUTICAL APPLICATION THEREOF

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Page/Page column 8-9, (2008/06/13)

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

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, (2008/06/13)

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

-

, (2008/06/13)

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

Oya, Masanao,Takahashi, Tomoko

, p. 2705 - 2707 (2007/10/02)

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).

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