61043-33-2

Usage

Uses

Used in Research Applications:
Z-ALA-ALA-LEU-PNA is used as a substrate for studying enzymatic activities, specifically for proteases that cleave after leucine residues. Its specificity and the presence of a fluorescent reporter group make it a valuable tool for identifying and characterizing protease enzymes.
Used in Drug Discovery and Development:
Z-ALA-ALA-LEU-PNA is used as a screening and profiling agent for protease inhibitors and modulators. Its applications in this field contribute to the advancement of drug discovery and development, particularly in the context of protease-targeted therapies.

InChI:InChI=1/C26H33N5O7/c1-16(2)14-22(25(34)29-20-10-12-21(13-11-20)31(36)37)30-24(33)17(3)27-23(32)18(4)28-26(35)38-15-19-8-6-5-7-9-19/h5-13,16-18,22H,14-15H2,1-4H3,(H,27,32)(H,28,35)(H,29,34)(H,30,33)/t17-,18-,22-/m0/s1

Upstream product

• 2483-51-4 N-[(benzyloxy)carbonyl]-L-alanyl-L-alanine methyl ester 
• 4178-93-2 (S)-2-amino-4-methyl-N-(4-nitrophenyl)valeramide 
• 16012-70-7 benzyloxycarbonyl-L-alanyl-L-alanine 

Downstream Products

• 54865-22-4 N-benzyloxycarbonyl-alanyl-alanyl-leucine 
• 100-01-6 4-nitro-aniline 

Relevant academic research and scientific papers

Peptide synthesis in organic media with the use of subtilisin 72 immobilized on a poly(vinyl alcohol) cryogel

Subtilisin 72 serine protease (EC 3.4.21.14) immobilized on a poly(vinyl alcohol) cryogel was used as a catalyst in the syntheses of N-protected peptide p-nitroanilides of the general formulas Z(or Boc)-Xaa-Phe-pNA (Xaa = Leu or Ala), Z-Ala-Xaa-Yaa-pNA (X

Proteinases immobilized on poly(vinyl alcohol) cryogel: Novel biocatalysts for peptide synthesis in organic media

Covalent immobilization of subtilisin and thermolysin on cryogel of poly(vinyl alcohol) was carried out. The biocatalysts obtained are characterized by high stability in water and in DMF-MeCN mixtures of various compositions The synthetic efficiency of im

SDS-subtilisin complex efficiently catalyzes synthesis of peptides in ethanol and 2-propanol

An enzymatic synthesis of tripeptide Z-Ala-Ala-Leu-pNA, tetrapeptides Z-Ala-Ala-P1-P1'-Xaa, where P1 = Leu, Trp, Met, Ala, Ile, Phe; P1'= Phe, Ala, Leu; Xaa = pNA, NH2, pentapeptides Z-Ala-Ala-Leu-Ala

Modified Proteases for Peptide Synthesis in Organic Media

We showed that modified proteases could catalyze synthesis of a wide variety of peptides of various lengths and structures both in solution and on solid phase in organic solvents. The following modified proteases were studied as catalysts for enzymatic peptide synthesis in polar organic solvents (acetonitrile, dimethylformamide, and ethanol): pepsin sorbed on celite, a noncovalent complex of subtilisin with sodium dodecylsulfate, and subtilisin or thermolysin covalently immobilized on a cryogel of polyvinyl alcohol. The use of the noncovalent complex of subtilisin with sodium dodecylsulfate and immobilized subtilisin is especially promising for the segment condensation of peptide fragments containing residues of trifunctional amino acids with unprotected ionogenic groups in side chains, such as Lys, Arg, His, Glu, and Asp.

Biocatalytic properties of thermolysin immobilized on polyvinyl alcohol cryogel

Preparations with different contents of thermolysin were obtained by the immobilization of the enzyme on granulated polyvinyl alcohol cryogel. Their activity and stability in an aqueous medium and in mixtures of polar organic solvents of different composition were investigated. The catalytic properties of the preparations in reactions of peptide bond formation were studied, and the optimal amount of the biocatalyst, the concentrations of initial reagents, and the ratios of organic solvents and water necessary for effective enzymatic peptide synthesis catalyzed by immobilized thermolysin were determined. A series of peptides of the general formula Z-Ala-Ala-Xaa-pNA, where Xaa = Leu, Ile, Phe, Val, or Ala, were synthesized, and the immobilized enzyme was shown to retain substrate specificity in an organic medium.

The synthesis of tri- and tetrapeptides catalyzed by subtilisin suspensions in organic solvents

The behavior of subtilisin 72 in some aprotic solvents (acetonitrile, dioxane, and tetrahydrofurane) was studied. The enzyme was shown to be partially soluble in tetrahydrofurane, but it is rendered profoundly inactive in this solution. In acetonitrile an

p-Nitroanilides of 3-carboxypropionyl-peptides. Their cleavage by elastase, trypsin, and chymotrypsin.

Fourteen 3-carboxypropionyl-tripeptide-p-nitroanilides of the general formula 3-carboxypropionyl-alanyl-alanyl-Y-p-nitroanilide (Y = glycine, norvaline, S-methylcysteine, valine, norleucine, S-ethylcysteine, methionine, leucine, isoleucine, phenylalanine, tyrosine, S-benzylcysteine, Calpha-phenylglycine, and proline) were synthesized and their cleavage by elastase, trypsin, and chymotrypsin (Km, kcat and kcat/Km) was determined. The significance of amino acid residues in the position of Y was evaluated firstly with respect to their structure (topographically), and secondly with respect to their free energy (thermodynamically). The alanine residue substrate was cleaved best by elastase, the phenylalanine substrate by chymotrypsin. Trypsin cleaved two substrates only, that is those containing a phenylalanine and a tyrosine residue. The optimum length of the elastolytic substrates was studied in a series of N-3-carboxypropionyl-(Ala)n-p-nitroanilides (n = 1, 2, 3, 4, 5), N-3-carboxypropionyl-(Gly)n-p-nitroanilides (n = 1, 2, 3), and in p-nitroanilides of fatty acids with two to seven carbon atoms. Elastase cleaved tri, tetra, and pentapeptides of alanine. p-Nitroanilides of the glycine series, as well as p-nitroanilides of fatty acids were not cleaved. 3-Carboxypropionyl-tetra-alanine-p-nitroanilide was the most suitable substrate so far found for elastase cleavage; it is not cleaved by trypsin nor chymotrypsin. The optimum distance between Y and the terminal anionic carboxyl residue was found to be 1.8 nm in elastolytic substrates.