926-77-2

Basic information

• Product Name: GLYCYL-DL-ALANINE
• Synonyms: DL-Alanine, N-glycyl-;GLY-DL-ALA;GLYCYL-DL-ALANINE;H-GLY-DL-ALA-OH;2-[(2-AMINOACETYL)AMINO]PROPANOIC ACID;N-glycyl-DL-alanine;Glycyl-Dl-Alanine,>99%;N-Glycyl-DL-ALPHA-alanine
• CAS NO: 926-77-2
• Molecular Formula: C₅H₁₀N₂O₃
• Molecular Weight: 146.14
• EINECS: 213-144-6
• Product Categories: Biochemistry;Oligopeptides;Peptide Synthesis
• Mol File: 926-77-2.mol

Chemical Properties

• Melting Point: 235 °C
• Boiling Point: 417.4±30.0 °C(Predicted)
• Appearance: /
• Density: 1.263±0.06 g/cm3(Predicted)
• Storage Temp.: −20°C
• PKA: 3.16±0.10(Predicted)
• Water Solubility: almost transparency in Water
• CAS DataBase Reference: GLYCYL-DL-ALANINE(CAS DataBase Reference)
• NIST Chemistry Reference: GLYCYL-DL-ALANINE(926-77-2)
• EPA Substance Registry System: GLYCYL-DL-ALANINE(926-77-2)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 926-77-2(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
GLYCYL-DL-ALANINE is used as a chiral reference compound for the development and optimization of methods for separating enantiomers. This is crucial in the pharmaceutical industry, as the different isomers of a drug can have different biological activities and potential side effects.
Used in Analytical Chemistry:
GLYCYL-DL-ALANINE is used as a test compound in liquid chromatography methods to evaluate the performance of chiral stationary phases and chiral mobile phase additives. This helps in the development of more efficient and accurate techniques for enantiomeric separation.
Used in Research and Development:
GLYCYL-DL-ALANINE serves as a model compound in research studies focused on understanding the behavior of chiral molecules and the mechanisms of enantioselective interactions. This knowledge can be applied to the design of new chiral drugs and the improvement of existing ones.

InChI:InChI=1/C5H10N2O3/c1-3(5(9)10)7-4(8)2-6/h3H,2,6H2,1H3,(H,7,8)(H,9,10)

Upstream product

• 23446-00-6 N-(N-benzyloxycarbonyl-glycyl)-DL-alanine 
• 14390-29-5 GlyGlyAla 
• 4703-35-9 N-(p-tosyl)glycylalanine 
• 10034-85-2 hydrogen iodide 
• 1190-32-5 monochloroacetyl-DL-alanine 
• 3695-73-6 Gly-L-Ala 
• 3695-73-6 glycyl-L-alanine 

Downstream Products

• 879008-63-6 N-(N-acetylthiocarbamoyl-glycyl)-alanine 
• 4526-77-6 3-methylpiperazine-2,5-dione 
• 83317-55-9 2-[(1-(4-Dimethylamino-phenyl)-3-(1,3-dioxo-1,3-dihydro-isoindol-2-yl)-2-{6-[2-(1,3-dioxo-1,3-dihydro-isoindol-2-yl)-acetoxy]-2,7-dimethoxy-1,4-dioxo-1,4-dihydro-carbazol-9-yl}-4-oxo-azetidine-2-carbonyl)-amino]-propionic acid 
• 83317-61-7 2-{[3-Amino-2-[6-(2-amino-acetoxy)-2,7-dimethoxy-1,4-dioxo-1,4-dihydro-carbazol-9-yl]-1-(4-dimethylamino-phenyl)-4-oxo-azetidine-2-carbonyl]-amino}-propionic acid; hydrochloride 
• 83334-59-2 2-[2-[(E)-4-Dimethylamino-phenylimino]-2-(6-hydroxy-2,7-dimethoxy-1,4-dioxo-1,4-dihydro-carbazol-9-yl)-acetylamino]-propionic acid 
• 60-35-5 acetamide 
• 62029-79-2 2-amino-N-ethyl-acetamide 
• 75-07-0 acetaldehyde 
• 14390-29-5 GlyGlyAla 

Relevant articles and documents

Kinetics of Amide and Peptide Cleavage by Alkaline Hydrogen Peroxide

(Equation Presented) The hydroperoxide anion cleaves unactivated amides and peptides although it is completely unreactive toward ethyl esters. The cleavage by HO2- proceeds faster than by OH- and involves additional routes with general acid assistance by H 2O2 and general base assistance by OH- and HO2-. Cleavage of polypeptides occurs at the N-terminal peptide bond.

Neighboring Residue Effects: Evidence for Intramolecular Assistance to Racemization or Epimerization of Dipeptide Residues

Dipeptides, their methyl esters, diketopiperazines (DKP), and N-substituted derivatives were racemized at high temperatures (approximately 120 deg C) in aqueous phosphate buffered solutions at pH values close to pH of maximum racemization (approximately 8).The racemization of the dipeptides Ala-Gly and Gly-Ala followed reversible first-order kinetics.The initial rate of racemization of DKP was very fast but soon slowed down, supposedly due to hydrolysis.The resulting rate was similar to that of the dipeptides.Esters of dipeptides followed racemization patterns similar to DKP.The racemization rate constants of the dipeptides studied were shown to be independent of the concentration of the dipeptide and the concentration of buffer.A carboxy-terminal proline residue greatly increased the rate of racemization (epimerization) of the amino-terminal residue.Increasing the basicity of the N-terminal amino acid residue increased the rate of racemization (or epimerization) of the C-terminal residue unless the C-terminal was sterically hindered as the Ile and Val.Decreasing the basicity of the N-terminal amino acid residue decreased racemization or epimerization for nonhindered C-terminal amino acids.These results support the influence of neighboring groups in the racemization or epimerization of dipeptides.DKP formation is a competing reaction allowing racemization or epimerization in dipeptides.Dipeptide racemization or epimerization is proposed to be the result of combination of intramolecular base assistance and DKP formation.