1948-31-8

Basic information

• Product Name: L-Alanyl-L-alanine
• Synonyms: H-ALA-ALA-OH;ALA-ALA;Alanine, N-L-alanyl-, L-;alpha-Alanylalanine;Dialanine;L-Alanine, N-L-alanyl-;N-L-alanyl-L-alanine;L-ALANYL-L-ALANINE extrapure
• CAS NO: 1948-31-8
• Molecular Formula: C₆H₁₂N₂O₃
• Molecular Weight: 160.17
• EINECS: 217-751-7
• Product Categories: Amino Acid Derivatives;99%
• Mol File: 1948-31-8.mol

Chemical Properties

• Melting Point: 280-285 °C(lit.)
• Boiling Point: 286.06°C (rough estimate)
• Flash Point: 197.3 °C
• Appearance: white crystalline powder
• Density: 1.208
• Vapor Pressure: 1.31E-07mmHg at 25°C
• Refractive Index: 1.4500 (estimate)
• Storage Temp.: -15°C
• Solubility: H2O: 0.1 g/mL, clear
• PKA: 3.16±0.10(Predicted)
• Stability: Stable. Incompatible with strong oxidizing agents.
• BRN: 1724813
• CAS DataBase Reference: L-Alanyl-L-alanine(CAS DataBase Reference)
• NIST Chemistry Reference: L-Alanyl-L-alanine(1948-31-8)
• EPA Substance Registry System: L-Alanyl-L-alanine(1948-31-8)

Safety Data

• Safety Statements: 24/25
• WGK Germany: 3
• Hazardous Substances Data: 1948-31-8(Hazardous Substances Data)

Usage

Uses

Used in Physicochemical Studies:
L-Alanyl-L-alanine is used as a model dipeptide for studying the effects of pH (protonation) on conformation. This helps researchers understand the behavior of larger peptides and proteins under different pH conditions.
Used in Pharmaceutical Research:
L-Alanyl-L-alanine can be used in the development of new drugs, as it serves as a building block for the synthesis of more complex peptide-based therapeutics.
Used in Nutritional Supplements:
As a dipeptide, L-Alanyl-L-alanine may be used in nutritional supplements to enhance protein synthesis and support muscle growth and repair.
Used in Cosmetics:
L-Alanyl-L-alanine can be used in the cosmetics industry for its potential skin-protective and moisturizing properties, as it may help improve skin hydration and maintain the skin's natural barrier function.
Used in Food Industry:
In the food industry, L-Alanyl-L-alanine can be used as a flavor enhancer, as it may contribute to the overall taste and texture of certain food products.
Used in Research and Development:
L-Alanyl-L-alanine is also used in research and development for the study of peptide synthesis, protein folding, and other related biotechnological applications.

InChI:InChI=1/C6H12N2O3/c1-3(7)5(9)8-4(2)6(10)11/h3-4H,7H2,1-2H3,(H,8,9)(H,10,11)/t3-,4-/m0/s1

Upstream product

• 128982-78-5 DL-2-(2-hydroxyimino-propionylamino)-propionic acid 
• 31654-38-3 N-(2-bromo-propionyl)-alanine 
• 5625-46-7 cyclo(-DL-Ala-DL-Ala-) 
• 17344-99-9 AlaOEt 
• 338-69-2 D-Alanine 
• 64-17-5 ethanol 
• 2392-63-4 N-pyruvoyl-alanine 
• 7732-18-5 water 
• 2835-06-5 phenylglycin 
• 7664-41-7 ammonia 
• 16012-70-7 benzyloxycarbonyl-L-alanyl-L-alanine 
• 82748-54-7 Ala-Ala-O-benzyl 
• 3886-07-5 Cbz-L-ala-L-ala-Cbz 
• 61043-41-2 H-Ala-Ala-Phe-p-nirtoanilide 

Downstream Products

• 5625-46-7 cyclo(-DL-Ala-DL-Ala-) 
• 2392-63-4 N-pyruvoyl-alanine 
• 22221-70-1 Cbz-HN-Ala-Ala 
• 106659-81-8 2-[2-(2-Cyano-ethylamino)-propionylamino]-propionic acid 
• 338-69-2 D-Alanine 
• 132402-91-6 Z-Glu-Ala-Ala-OH 
• 132402-89-2 Mal-Tyr-Ala-Ala-OH 
• 132402-90-5 Mal-Phe-Ala-Ala-Ala-OH 
• 87184-25-6 Boc-DL-m-FPhe-L-Ala-L-Ala 
• 5845-61-4 cyclo(L-Ala-L-Ala) 
• 13139-27-0 L-α-N-Cbz-alaninamide 
• 27317-69-7 N-tert-butoxycarbonyl-L-alanyl-L-alanine 

Relevant articles and documents

Mechanochemical Prebiotic Peptide Bond Formation**

The presence of amino acids on the prebiotic Earth, either stemming from endogenous chemical routes or delivered by meteorites, is consensually accepted. Prebiotically plausible pathways to peptides from inactivated amino acids are still unclear as most oligomerization approaches rely on thermodynamically disfavored reactions in solution. Now, a combination of prebiotically plausible minerals and mechanochemical activation enables the oligomerization of glycine at ambient temperature in the absence of water. Raising the reaction temperature increases the degree of oligomerization concomitantly with the formation of a commonly unwanted cyclic glycine dimer (DKP). However, DKP is a productive intermediate in the mechanochemical oligomerization of glycine. The findings of this research show that mechanochemical peptide bond formation is a dynamic process that provides alternative routes towards oligopeptides and establishes new synthetic approaches for prebiotic chemistry.

A dynamic combinatorial library for biomimetic recognition of dipeptides in water

Small peptides are involved in countless biological processes. Hence selective binding motifs for peptides can be powerful tools for labeling or inhibition. Finding those binding motifs, especially in water which competes for intermolecular H-bonds, poses an enormous challenge. A dynamic combinatorial library can be a powerful method to overcome this issue. We previously reported artificial receptors emerging form a dynamic combinatorial library of peptide building blocks. In this study we aimed to broaden this scope towards recognition of small peptides. Employing CXC peptide building blocks, we found that cyclic dimers of oxidized CFC bind to the aromatic peptides FF and YY (K ≈ 229-702 M-1), while AA binds significantly weaker (K ≈ 65-71 M-1).

Effect of high hydrostatic pressure on prebiotic peptide synthesis

Prebiotic peptide synthesis is a central issue concerning life's origins. Many studies considered that life might come from Hadean deep-sea environment, that is, under high hydrostatic pressure conditions. However, the properties of prebiotic peptide formation under high hydrostatic pressure conditions have seldom been mentioned. Here we report that the yields of dipeptides increase with raised pressures. Significantly, effect of pressure on the formation of dipeptide was obvious at relatively low temperature. Considering that the deep sea is of high hydrostatic pressure, the pressure may serve as one of the key factors in prebiotic peptide synthesis in the Hadean deep-sea environment. The high hydrostatic pressure should be considered as one of the significant factors in studying the origin of life.

Pressure-induced oligomerization of alanine at 25 °C

Pressure-induced oligomerization was found from high-pressure experiments at 25 °C on alanine powder soaked in its saturated aqueous solution. The oligomerization to alanylalanine occurred at 5 GPa. The maximum yields of alanylalanine and trialanine were, respectively, 1.1 × 10-3 and 1.3 × 10-4 at 11 GPa.

Rapid, effective deprotection of tert-butoxycarbonyl (Boc) amino acids and peptides at high temperatures using a thermally stable ionic liquid

A method for high temperature Boc deprotection of amino acids and peptides in a phosphonium ionic liquid is described. The ionic liquid had low viscosity, high thermal stability and demonstrated a beneficial effect. The study extended the possibility for extraction of water soluble polar organic molecules using ionic liquids. Trace water significantly improved product purity and yield, while only 2 equiv. TFA led to deprotection within 10 min. The trityl group was also deprotected.

Coupling-Reagent-Free Synthesis of Dipeptides and Tripeptides Using Amino Acid Ionic Liquids

A general method for the synthesis of dipeptides has been developed, which does not require any coupling reagents. This method is based on the reaction of readily available HCl salts of amino acid methyl esters with tetrabutylphosphonium amino acid ionic liquids. The isolation procedure of stepwise treatment with AcOH is easy to carry out. The method was extended to the synthesis of tripeptide, tyrosyl-glycyl-glycine, present in IMREG-1, also.

Epimerization of cyclic alanyl-alanine in basic solutions

Alanine anhydrides (Cyclo-(Ala-Ala)) are the simplest dipeptides that have two chiral centers and three diastereomers: Cyclo-(L-Ala-L-Ala), Cyclo-(D-Ala-D-Ala), and Cyclo-(L-Ala-D-Ala). Analysis of the epimerization of these peptides may throw light on the development of homochirality in proteins. We show that the epimerization rate of Cyclo-(L-Ala-L-Ala) and Cyclo-(D-Ala-D-Ala) is higher than that of Cyclo-(L-Ala-D-Ala), while the ring-opening rates of Cyclo-(L-Ala-L-Ala) and Cyclo-(D-Ala-D-Ala) arelower than that of Cyclo-(L-Ala-D-Ala) in basic aqueous solutions. The total reaction resulted in the preferred stability of Cyclo-(L-Ala-L-Ala) and Cyclo-(D-Ala-D-Ala) to Cyclo-(D-Ala-L-Ala).

The dimethylsulfoxonium methylide as unique reagent for the simultaneous deprotection of amino and carboxyl function of N-Fmoc-α-amino acid and N-Fmoc-peptide esters

The dimethylsulfoxonium methylide is described as a unique and useful reagent for the simultaneous deprotection of amino and carboxyl function of N-Fmoc-α-amino acid and N-Fmoc-peptide esters. The new methodology was applied successfully both to solution- and solid-phase peptide synthesis. The adopted methodology was extended successfully also to peptides containing amino acids bearing acid-sensitive protecting group in side chains. Furthermore no measurable epimerization was observed in the deprotection reaction of N-Fmoc-dipeptide methyl esters with dimethylsulfoxonium methylide.

Oligomerization of glycine and alanine on metal(II) octacynaomolybdate(IV): Role of double metal cyanides in prebiotic chemistry

Condensation reactions of amino acid (glycine and alanine) on the surface of metal(II) octacyanomolybdate( IV) (MOCMo) complexes are investigated using highperformance liquid chromatography (HPLC) and electron spray ionizations-mass spectroscopy (ESI-MS). The series of MOCMo have been synthesized and the effect of outer sphere metal ions present in the MOCMo on the oligomerization of glycine and alanine at different temperature and time found out. Formation of peptides was observed to start after 7 days at 60°C. Maximum yield of peptides was found after 35 days at 90°C. It has been found that zinc(II) octacyanomolybdate( IV) and cobalt(II) were the most effective metal cations present in outer sphere of the MOCMo for the production of high yield of oligomerized products. Surface area of MOCMo seems to play dominating parameter for the oligomerization of alanine and glycine. The results of the present study reveal the role of MOCMo in chemical evolution for the oligomerization of biomolecules. Springer-Verlag 2012.

Process For Producing Dipeptides or Dipeptide Derivatives

The present invention provides a process for producing a dipeptide or a dipeptide derivative by using a protein having the activity to form the dipeptide or dipeptide derivative from one or more kinds of amino acids or amino acid derivatives, or a culture of cells having the ability to produce the protein or a treated matter of the culture as a enzyme source, which comprise; allowing the enzyme source, one or more kinds of amino acids or amino acid derivatives and ATP to be present in an aqueous medium; allowing the dipeptide or dipeptide derivative to form and accumulate in the medium; and recovering the dipeptide or dipeptide derivative from the medium.