50439-35-5

Basic information

• Product Name: BOC-ALA-ALA-PNA
• Synonyms: N-BOC-L-ALA-ALA-P-NITROANILIDE;BOC-L-ALANYL-ALANINE P-NITROANILIDE;BOC-ALA-ALA-PNA;BOC-ALA-ALA-P-NITROANILIDE;N-T-BOC-ALA-ALA P-NITROANILIDE);N-(tert-butoxycarbonylmethyl)alanine-alanine-nitroanilide
• CAS NO: 50439-35-5
• Molecular Formula: C₁₇H₂₄N₄O₆
• Molecular Weight: 380.4
• Mol File: 50439-35-5.mol

Chemical Properties

• Boiling Point: 654.8±50.0 °C(Predicted)
• Appearance: /
• Density: 1.259±0.06 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 11.34±0.46(Predicted)
• CAS DataBase Reference: BOC-ALA-ALA-PNA(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-ALA-ALA-PNA(50439-35-5)
• EPA Substance Registry System: BOC-ALA-ALA-PNA(50439-35-5)

Safety Data

• Hazardous Substances Data: 50439-35-5(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
BOC-ALA-ALA-PNA is used as a building block for the assembly of peptides and peptidomimetics for drug discovery and development. Its protective BOC group and PNA moiety make it a valuable component in the synthesis of novel therapeutic agents.
Used in Biochemical Research:
BOC-ALA-ALA-PNA is used as a research tool in biochemical studies, where its PNA moiety allows for the investigation of peptide-nucleic acid interactions and the development of new diagnostic techniques.
Used in Materials Science:
BOC-ALA-ALA-PNA is used in the development of new materials with unique properties, such as self-assembling systems and stimuli-responsive materials, due to its peptide and PNA components.

Upstream product

• 15761-38-3 L-N-Boc-Ala 
• 1668-13-9 L-alanine-p-nitroanilide 
• 181117-99-7 tert-butyloxycarbonylalanine 4-guanidinophenyl ester 
• 221017-30-7 C₃₅H₃₆N₄O₈ 
• 221017-26-1 C₃₅H₃₆N₄O₈ 
• 221017-34-1 C₃₅H₃₆N₄O₈ 
• 221017-22-7 C₃₅H₃₆N₄O₈ 
• 1026750-87-7 C₃₂H₃₆N₄O₈ 

Downstream Products

• 223753-63-7 Boc-Val-ψ-(CH2-NH)-Ala-Ala-pNA 

Relevant articles and documents

Application of various inverse substrates to thrombin-catalyzed peptide synthesis

Thrombin-catalyzed peptide synthesis has been studied using nine series of 'inverse substrates' i.e., pamidinophenyl, p- and m-guanidinophenyl, p- and m-(guanidinomethyl)phenyl, and four position isomers of guanidinonaphthyl esters derived from N(α)-(tert

Atlantic cod trypsin-catalyzed peptide synthesis with inverse substrates as acyl donor components

Atlantic cod trypsin-catalyzed peptide synthesis has been studied by using p-amidino- and p-guanidinophenyl esters of N-(tert-butyloxycarbonyl)amino acid as acyl donor components. The reaction temperature was optimized at 0 °C. The method was shown to be successful as effectively for synthesizing the peptide and useful for preparing dipeptide between D-amino acid with D-amino acid and β-amino acid with β-amino acid, respectively. The enzymatic hydrolysis of the resulting products was negligible.

Trypsin-catalyzed synthesis of dipeptide containing α-aminoisobutylic acid using p- and m-(amidinomethyl)phenyl esters as acyl donor

Two series of inverse substrates, p- and m-(amidinomethyl)phenyl esters derived from N-(tert-butyloxycarbonyl) amino acid, were prepared as acyl donor components for enzymatic peptide synthesis. They were found to be readily coupled with an acyl acceptor such as L-alanine p-nitroanilide to produce dipeptide. An α-aminoisobutyric acid containing dipeptide was especially obtained in satisfactory yield. Streptomyces griseus trypsin was a more efficient catalyst than the bovine trypsin. The optimum condition for the coupling reaction was studied by changing the organic solvent, pH, and acyl acceptor concentration. It was found that the enzymatic hydrolysis of the resulting product was negligible.

The structural requirements for an inverse substrate for enzymatic peptide synthesis: Position isomers of guanidinonaphthyl esters as the acyl donor component

Four series of inverse substrates, position isomers of guanidinonaphthyl esters derived from N-(tert-butyloxycarbonyl)amino acid, were prepared as acyl donor components for trypsin-catalyzed peptide synthesis. The kinetic behavior of these synthetic inver

Enzymatic peptide synthesis with p-guanidinophenyl and p- (guanidinomethyl)phenyl esters as acyl donors

Two series of 'inverse substrates', N-Boc-amino acid p-guanidinophenyl and p-(guanidinomethyl)phenyl esters, were prepared as acyl donor components for enzymatic peptide synthesis. The kinetic behavior of these esters toward bovine and Streptomyces griseus (SG) trypsin was analyzed. The spatial requirement of the active site of these enzymes for catalytic efficiency is discussed based on the steric characteristics of the substrates. These substrates were found to couple readily with amino acid p-nitroanilides to produce peptides. SG trypsin was the most efficient catalyst among the enzymes tested (bovine, porcine, and SG trypsin).

Methyltrypsin-catalyzed peptide coupling: Comparison of alkyl ester and guanidinophenyl ester derivatives as acyl donor component

Methyltrypsin-catalyzed peptide synthesis has been studied by using conventional alkyl ester and p-guanidinophenyl ester derivatives of α-amino acid as the acyl donor component. They were found to be coupled with α- amino acid derivatives (acyl acceptor component) to produce dipeptide. The behavior of methyltrypsin toward both the substrates has been studied.

Trypsin-catalyzed peptide synthesis with various p-guanidinophenyl esters as acyl donors

Trypsin-catalyzed peptide synthesis has been studied by using p- guanidinophenyl esters of N(α)-(tert-butyloxycarbonyl)amino acid and peptide as acyl donor components. The reaction conditions were optimized for organic solvents, pH, and concentration of a

Amino acids and peptides. XXXIX. Synthesis of iNoc-Gln-Val-Val-Ala-Ala-pNA and its action on thiol proteinases

Based on the results of X-ray analysis of the complex between Suc-Gln-Val-Val-Ala-Ala-pNA, a fairly potent thiol proteinase inhibitor, and papain, iNoc-Gln-Val-Val-Ala-Ala-pNA was designed and prepared and its inhibitory activity against thiol proteinases