205252-36-4

Basic information

• Product Name: H-D-ALA-GLN-OH
• Synonyms: D-ALANINE-L-GLUTAMINE;H-D-ALA-GLN-OH;H-D-Ala-L-Glu-NH2;(S)-5-amino-2-((R)-2-aminopropanamido)-5-oxopentanoic
• CAS NO: 205252-36-4
• Molecular Formula: C8H15N3O4
• Molecular Weight: 217.22
• Mol File: 205252-36-4.mol

Chemical Properties

• Boiling Point: 615.4±55.0 °C(Predicted)
• Appearance: /
• Density: 1.305±0.06 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 3.12±0.10(Predicted)
• CAS DataBase Reference: H-D-ALA-GLN-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-D-ALA-GLN-OH(205252-36-4)
• EPA Substance Registry System: H-D-ALA-GLN-OH(205252-36-4)

Safety Data

• Hazardous Substances Data: 205252-36-4(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-D-ALA-GLN-OH is used as a synthetic compound for the activation of natural killer (NK) cells. It plays a crucial role in the immune system by enhancing the function of NK cells, which are essential for the body's defense against cancer and viral infections.
Used in Synthesis of Dipeptides:
H-D-ALA-GLN-OH is used as a building block in the synthesis of dipeptides, which are short chains of amino acids linked by peptide bonds. These dipeptides can have various biological activities and can be used for different purposes, such as drug development and therapeutic applications.

Upstream product

• 159141-33-0 N-(α-chloro)propionylglutamine 
• 90770-50-6 L-Alanyl-<γ-methyl>-L-glutamat 
• 4652-65-7 (S)-2-Benzyloxycarbonylamino-pentanedioic acid 5-methyl ester 
• 96789-24-1 α-p-Nitro-benzyl-γ-methyl-L-glutamat 
• 56-85-9 L-glutamine 
• 1142-20-7 N-Cbz-Ala 
• 5872-22-0 N-pivaloylalanine 
• 2491-20-5 L-alanine methyl ester hydrochloride 
• 159141-33-0 N-(α-chloro)propionyl-L-glutamine 
• 159141-33-0 2-chloropropionyl-L-glutamine 
• 101896-82-6 Carbobenzoxy-L-alanyl-<α-p-nitro-benzyl,γ-methyl>-L-glutamat 
• 910908-63-3 N-Carbobenzoxy-<α-p-nitro-benzyl,γ-methyl>-L-glutamat 
• 5959-95-5 D-Glutamin 
• 21467-17-4 Z-Ala-Gln-OH 

Relevant articles and documents

Gene cloning and characterization of α-amino acid ester acyl transferase in empedobacter brevis ATCC14234 and Sphingobacterium siyangensis AJ2458

The gene encoding α-amino acid ester acyl transferase (AET), the enzyme that catalyzes the peptideforming reaction from amino acid methyl esters and amino acids, was cloned from Empedobacter brevis ATCC14234 and Sphingobacterium siyangensis AJ2458 and expressed in Escherichia coli. This is the first report on the aet gene. It encodes a polypeptide composed of 616 (ATCC14234) and 619 (AJ2458) amino acids residues. The Vmax values of these recombinant enzymes during the catalysis of L-alanyl-L-glutamine formation from L-alanine methylester and L-glutamine were 1,010 U/mg (ATCC14234) and 1,154 U/mg (AJ2458). An amino acid sequence similarity search revealed 35% (ATCC14234) and 36% (AJ2458) identity with an α-amino acid ester hydrolase from Acetobacter pasteurianus, which contains an active-site serine in the consensus serine enzyme motif, GxSYxG. In the deduced amino acid sequences of AET from both bacteria, the GxSYxG motif was conserved, suggesting that AET is a serine enzyme.

ALANYL GLUTAMINE COMPOUND AND PREPARATION METHOD THEREOF

A process for preparing a pure alanylglutamine comprises the steps of: 1) reacting N-(α-chloro)-propionyl-glutamine and hydrazine compound to obtain an alanylglutamine crude product; 2) mixing anhydrous methanol and the alanylglutamine crude product to provide a filter cake; 3) dissolving the filter cake in water, heating, adding ethanol, and cooling to yield the pure alanylglutamine.

Process of producing ala-gln dipeptide

A synthesis method of alanyl-glutamine includes the steps of: The N-terminal protected alanine reacts with triphenylphosphine and hexachloroethane in organic solvent to form active ester, the active ester reacts with glutamine in a solution mixture containing organic solvent and aqueous solution of inorganic base, the resultant mixture is acidified with inorganic acid, and then the N-terminal protecting group is removed. In this method, the raw materials are cheap, the synthesis technique is simple, no disposals of separation and purification are needed, the product is easy to be separated and purified, the toxicities of all the reagents used in the course of production are minimal, it is advantageous to environment protection.

Recovery of ammonia in the dipeptide manufacturing processes

An example of an improvement in recovering ammonia in a dipeptide manufacturing process is described. The synthetic method, which makes use of the ammonolysis reaction, has been studied and found to produce dipeptides of satisfactory quality in high yield on a large scale. However, the treatment of unreacted ammonia in the ammonolysis reaction caused a reduction in the productivity and increased the production cost during actual manufacture. Therefore, a method to recover the unreacted ammonia has been investigated through simulations and trial runs using model solutions. Consequently, the modified process provided an improvement in the productivity and cost savings. In addition, the recovered ammonia could possibly be used for recycling. It was verified in a lab experiment that the reused ammonia did not lower the quality of the dipeptide.

Process research and development of L-alanyl-L-glutamine, a component of parenteral nutrition

A large-scale manufacturing method of L-alanyl-L-glutamine used for a component of parenteral nutrition has been studied. The method consisted of a reaction of D-2-chloro- or D-2-bromopropionic acid with thionyl chloride and Schotten-Baumann reaction with L-glutamine followed by ammonolysis reaction. The intermediate D-2-chloropropionyl-L-glutamine was found to be more stable than its bromo analogue. In the ammonolysis reaction, the former intermediate needed a higher reaction temperature, but the by-products produced had little effect on the quality of the final product. The structures of the by-products were conjectured mainly by mass spectrometry and they were removed by anion resin treatment and recrystallization.

Cosmetic composition

A composition suitable for topical application to mammalian skin and hair for inducing, maintaining or increasing hair growth comprises a hair growth promoter chosen from glutamine derivatives and salts thereof. The composition preferably also comprises an activity enhancer which may be chosen from hair growth stimulants, penetration enhancers and cationic polymers.

Process for the production of glutamine derivatives

Improved methods for synthesizing glutamine-containing peptides, involving an active ester method between a protected, C-terminal activated amino acid or a protected, C-terminal activated peptide, and unprotected glutamine in the presence of a weak base, are disclosed.

Human interferon-related peptides, antigens, antibodies and process for preparing the same

Human interferons related peptides and derivatives thereof, antigens, antibodies prepared therefrom, immobilized antibodies to be used for affinity chromatography, and novel method for assaying human interferons by using said affinity chromatography.