52299-14-6

Usage

Uses

Used in Enzyme Activity Screening:
SUC-ALA-ALA-ALA-PNA is used as a substrate for screening elastase activity in various biological samples, including lyophilized earthworm fibrinolytic enzymes, sheep milk, and honeybee inhibitors in serine protease inhibition assays. The substrate's chromogenic properties enable the detection and quantification of elastase activity, making it a valuable tool in research and diagnostic applications.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, SUC-ALA-ALA-ALA-PNA serves as a crucial component in the development and testing of new drugs targeting serine proteases. By monitoring the enzyme activity using this substrate, researchers can evaluate the efficacy and specificity of potential therapeutic agents, ultimately contributing to the advancement of novel treatments for various diseases.
Used in Research and Diagnostics:
SUC-ALA-ALA-ALA-PNA is also utilized in research and diagnostic laboratories to study the function and regulation of serine proteases. The substrate's ability to produce a colorimetric signal upon enzymatic cleavage facilitates the measurement of enzyme activity in various experimental setups, including high-throughput screening assays and kinetic studies.

InChI:InChI=1/C19H25N5O8/c1-10(20-15(25)8-9-16(26)27)17(28)21-11(2)18(29)22-12(3)19(30)23-13-4-6-14(7-5-13)24(31)32/h4-7,10-12H,8-9H2,1-3H3,(H,20,25)(H,21,28)(H,22,29)(H,23,30)(H,26,27)/t10-,11-,12-/m0/s1

Upstream product

• 108-30-5 succinic acid anhydride 
• 60354-61-2 L-Ala-L-Ala-L-Ala-pNA 
• 2483-52-5 benzyl ((S)-1-(((S)-1-hydrazinyl-1-oxopropan-2-yl)amino)-1-oxopropan-2-yl)carbamate 
• 1668-13-9 L-alanine-p-nitroanilide 
• 52357-40-1 Z-Ala-Ala-Ala-pNA 

Downstream Products

• 100-01-6 4-nitro-aniline 
• 1668-13-9 L-alanine-p-nitroanilide 
• 141509-27-5 N-succinyl-Ala-Ala 

Relevant academic research and scientific papers

ROLE OF AMINO ACID RESIDUES IN CHROMOGENIC SUBSTRATES CLEAVED BY PANCREATIC ELASTASE

Anionic chromogenic substrates, 3-carboxypropionyl tripeptide p-nitroanilides modified with glycine, β-alanine, alanine, leucine, and proline in positions P1, P2, and P3 were synthesized.The substrates were digested with pancreatic elastase and the values of Km, kcat, and kcat/Km were determined.Alanine plays a decisive role in position P1, substrates with glycine or β-alanine in this position are not cleaved.The substitution in P2 is dominant for proline; next follow alanine, leucine, and glycine.The substitution in P3 is the least specific one.

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.