Suc-ala-ala-pro-glu-pna is a chromogenic tetrapeptide containing a p-nitroaniline reporter group that monitors enzymatic cleavage. The sequence provides a defined recognition motif for catalytic analysis. Researchers employ it in specificity mapping, kinetic assays, and structural-functional correlation. Its succinylation enhances substrate solubility.
CAT No: R2250
CAS No:108929-37-9
Synonyms/Alias:SUC-ALA-ALA-PRO-GLU-PNA;108929-37-9;Suc-AAPE-pNA;(4S)-4-[[(2S)-1-[(2S)-2-[[(2S)-2-(3-carboxypropanoylamino)propanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]-5-(4-nitroanilino)-5-oxopentanoic acid;MFCD00238356;HY-P4482;DA-58146;FS110775;CS-0654438;(S)-4-((S)-1-((S)-2-((S)-2-(3-carboxypropanamido)propanamido)propanoyl)pyrrolidine-2-carboxamido)-5-(4-nitrophenylamino)-5-oxopentanoic acid;
Suc-ala-ala-pro-glu-pna is a synthetic peptide substrate widely utilized in biochemical research to investigate the activity and specificity of proteolytic enzymes, particularly those within the serine protease family. Structurally, it features a peptide backbone composed of alanine, proline, and glutamic acid residues, N-terminally protected with a succinyl group and C-terminally linked to p-nitroanilide (pNA). This design enables colorimetric detection upon enzymatic cleavage, making it a valuable tool for kinetic studies and enzyme characterization. Its defined sequence and chromogenic leaving group facilitate precise monitoring of protease activity, supporting a range of applications in enzymology, drug discovery, and molecular biology.
Enzyme Activity Assays: In the context of protease research, Suc-ala-ala-pro-glu-pna serves as a chromogenic substrate that releases p-nitroaniline upon enzymatic hydrolysis. The liberated pNA can be quantitatively measured spectrophotometrically, providing a straightforward and sensitive method for assessing protease activity. This enables researchers to determine enzyme kinetics, substrate specificity, and catalytic efficiency under various experimental conditions, making the peptide substrate essential for routine and high-throughput screening of protease function.
Inhibitor Screening: The substrate's well-defined cleavage mechanism makes it highly suitable for evaluating the efficacy of protease inhibitors. By monitoring changes in the rate of pNA release in the presence of candidate compounds, scientists can quantitatively assess inhibitor potency and selectivity. This application is particularly valuable in pharmaceutical research, where the identification and optimization of enzyme inhibitors are critical steps in the development of new therapeutic agents targeting proteolytic pathways.
Enzyme Specificity Profiling: Suc-ala-ala-pro-glu-pna is commonly employed to probe the substrate preferences of various serine proteases, such as elastase or chymotrypsin-like enzymes. By incorporating specific amino acid sequences, the substrate enables detailed mapping of enzyme-substrate recognition motifs. These studies provide insights into protease function, substrate binding interactions, and the structural determinants of specificity, supporting both fundamental enzymology and applied research in protein engineering.
Biochemical Pathway Elucidation: The substrate's ability to report on proteolytic activity in complex mixtures allows for its use in dissecting biochemical pathways involving serine proteases. Researchers can employ it to monitor enzyme activity in cell lysates, tissue extracts, or reconstituted systems, facilitating the identification of active enzymes and their roles within larger biological networks. This contributes to a deeper understanding of regulatory mechanisms and protease-mediated processes in diverse biological contexts.
Analytical Method Development: The reliable colorimetric response provided by Suc-ala-ala-pro-glu-pna supports its use in the development and validation of analytical assays for protease quantification. Laboratories can standardize protocols for routine enzyme monitoring, quality control, and process optimization in research and industrial settings. Its consistent performance and ease of detection make it a preferred choice for establishing robust, reproducible methodologies in protease analysis.
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