71067-42-0

Basic information

• Product Name: H-ALA-PRO-OME HCL
• Synonyms: H-ALA-PRO-OME HCL;H-Ala-Pro-OMe;(S)-Methyl 1-((S)-2-aMinopropanoyl)pyrrolidine-2-carboxylate hydrochloride;L-Proline, L-alanyl-, methyl ester, hydrochloride (1:1);L-Alanyl-L-proline methyl ester hydrochloride
• CAS NO: 71067-42-0
• Molecular Formula: C₉H₁₇N₂O₃*Cl
• Molecular Weight: 236.7
• Mol File: 71067-42-0.mol

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-ALA-PRO-OME HCL(CAS DataBase Reference)
• NIST Chemistry Reference: H-ALA-PRO-OME HCL(71067-42-0)
• EPA Substance Registry System: H-ALA-PRO-OME HCL(71067-42-0)

Safety Data

• Hazardous Substances Data: 71067-42-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research and Development:
H-ALA-PRO-OME HCL is used as a building block for the synthesis of peptides and the development of new pharmaceutical compounds. Its protective Boc group ensures controlled peptide synthesis, preventing side reactions that could affect the final product's efficacy and purity.
Used in Peptide Synthesis:
In the field of peptide synthesis, H-ALA-PRO-OME HCL is used as a protected amino acid. The Boc group on the nitrogen atom of L-alanine allows for the stepwise addition of other amino acids in a controlled manner, which is essential for the creation of specific peptide sequences with desired biological activities.
Used in Drug Design and Medicinal Chemistry:
H-ALA-PRO-OME HCL is utilized in drug design and medicinal chemistry as a component of potential therapeutic agents. Its role in the synthesis of bioactive peptides and other pharmaceuticals contributes to the discovery and development of new treatments for various diseases and conditions.
Used in Chemical Synthesis Education:
In educational settings, H-ALA-PRO-OME HCL can be used as a teaching aid to demonstrate the principles of peptide synthesis and the importance of protecting groups in organic chemistry and biochemistry. This helps students understand the practical applications of theoretical concepts in real-world scenarios.

Upstream product

• 33300-71-9 (S)-methyl 1-((S)-2-((tert-butoxycarbonyl)amino)propanoyl)pyrrolidine-2-carboxylate 
• 2133-40-6 L-proline methyl ester monohydrochloride 
• 2577-48-2 methyl (2S)-pyrrolidine carboxylate 

Downstream Products

• 86704-67-8 benzyloxycarbonylphenylalanylalanylproline methyl ester 
• 109953-29-9 N-t-butoxycarbonyl-L-prolyl-L-alanyl-L-prolyl-α-aza-alanine benzyl ester 
• 103972-56-1 N^α-furylacryloyltyrosylalanylproline methyl ester 
• 103972-54-9 N^α-furylacryloylphenylalanylalanylproline methyl ester 
• 99572-75-5 N^α-furylacryloylphenylalanylalanylproline 
• 36357-32-1 (3S,8aS)-3-methylhexahydropyrrolo[1,2-a]pyrazine-1,4-dione 
• 144647-60-9 (S)-1-[(S)-2-((2S,3R)-3,7-Bis-benzyloxycarbonylamino-2-hydroxy-heptanoylamino)-propionyl]-pyrrolidine-2-carboxylic acid methyl ester 

Relevant articles and documents

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.