Suc-Ala-Ala-Pro-Lys-pNA is a chromogenic substrate containing a lysine-p-nitroanilide reporter that enables measurement of trypsin-like protease activity. The succinyl cap regulates charge and substrate orientation. Researchers quantify p-nitroaniline release to determine catalytic constants. Applications include enzyme-screening assays, mechanistic studies, and protease-specificity analysis.
CAT No: R2375
CAS No:108929-39-1
Synonyms/Alias:Suc-Ala-Ala-Pro-Lys-pNA;108929-39-1;Suc-AAPK-pNA;4-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S)-6-amino-1-(4-nitroanilino)-1-oxohexan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid;MFCD00238358;HY-P4484;4-((S)-1-((S)-1-((S)-2-((S)-6-amino-1-(4-nitrophenylamino)-1-oxohexan-2-ylcarbamoyl)pyrrolidin-1-yl)-1-oxopropan-2-ylamino)-1-oxopropan-2-ylamino)-4-oxobutanoic acid;DA-58147;FS110776;CS-0654443;
Suc-Ala-Ala-Pro-Lys-pNA, also known as N-Succinyl-Ala-Ala-Pro-Lys-para-nitroanilide, is a synthetic chromogenic peptide substrate widely utilized in biochemical and enzymatic research. Characterized by its well-defined amino acid sequence and the presence of a para-nitroanilide (pNA) chromophore, this compound enables sensitive detection of proteolytic activity, especially for enzymes with trypsin-like specificity. The succinylation at the N-terminus enhances its solubility and stability, making it suitable for a variety of in vitro applications. Its ability to release p-nitroaniline upon enzymatic cleavage allows for straightforward spectrophotometric quantification, providing researchers with a reliable tool for kinetic analysis and functional studies involving serine proteases and related enzymes.
Enzyme Kinetics Assays: Suc-Ala-Ala-Pro-Lys-pNA serves as an indispensable substrate for quantifying the activity of serine proteases, particularly those exhibiting trypsin-like specificity. When these enzymes cleave the peptide bond adjacent to the lysine residue, the pNA moiety is released, producing a distinct yellow color measurable at 405 nm. This chromogenic response allows for real-time monitoring of enzyme kinetics, enabling precise measurement of reaction rates and detailed characterization of catalytic mechanisms. The substrate's high specificity and sensitivity facilitate the determination of Michaelis-Menten parameters, making it a preferred choice for enzyme activity profiling and inhibitor screening in academic and pharmaceutical research settings.
Protease Inhibitor Screening: In drug discovery and biochemical research, the chromogenic peptide is frequently employed to evaluate the efficacy of protease inhibitors. By introducing candidate inhibitors into assay systems containing the substrate and target enzyme, researchers can monitor changes in the rate of pNA release, thereby quantifying inhibitory potency. This application is critical for identifying and optimizing molecules that modulate protease activity, which has implications for therapeutic development and understanding protease regulation in physiological and pathological contexts. The ease of use and reproducibility of assays involving Suc-Ala-Ala-Pro-Lys-pNA streamline the screening process, accelerating the identification of promising inhibitor compounds.
Quality Control in Enzyme Production: The peptide substrate plays a significant role in quality assurance protocols for commercial and laboratory-grade protease preparations. By providing a rapid, quantifiable readout of enzyme activity, it enables manufacturers and researchers to validate the potency and consistency of protease batches. This is particularly important in the production of enzymes for research, industrial, or diagnostic applications, where activity levels must be tightly controlled to ensure reliable performance. The substrate's robust response and compatibility with automated platforms further enhance its utility in routine quality control workflows.
Functional Characterization of Mutant Enzymes: Suc-Ala-Ala-Pro-Lys-pNA is frequently utilized to investigate the functional properties of engineered or naturally occurring protease variants. By comparing the cleavage rates of wild-type and mutant enzymes using this substrate, researchers can elucidate the effects of specific amino acid substitutions on substrate recognition, catalytic efficiency, and overall enzyme function. Such studies are instrumental in protein engineering, structure-function analysis, and the exploration of disease-associated mutations, providing insights that inform the rational design of novel protease variants with tailored properties.
Biochemical Education and Training: The chromogenic properties and straightforward assay format of the peptide make it an excellent teaching tool in biochemical education. Students and trainees can gain practical experience in enzyme kinetics, data analysis, and assay optimization by working with this substrate in laboratory courses and training workshops. Its clear visual readout and reproducible results help reinforce fundamental concepts in enzymology and analytical biochemistry, fostering a deeper understanding of protease function and assay development.
Research into protease-substrate interactions: Suc-Ala-Ala-Pro-Lys-pNA also supports advanced studies of substrate specificity and enzyme-substrate interactions, offering a model system for dissecting the molecular determinants of proteolytic cleavage. By systematically modifying the peptide sequence or testing it alongside related substrates, scientists can map enzyme preferences and probe the structural basis of substrate recognition. These investigations contribute to the broader understanding of protease biology and inform the development of novel substrates and inhibitors for research and therapeutic applications.
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