N-Methoxysuccinyl-Ala-Ala-Pro-Val p-Nitroanilide incorporates a protected substrate motif with a p-nitroanilide reporter for detecting serine protease activity. Proline imposes a turn-like constraint that modulates recognition. Researchers quantify cleavage via chromogenic release. Applications include protease-characterization studies, inhibitor testing, and kinetic method development.
CAT No: PI-027
CAS No:70967-90-7
Synonyms/Alias:70967-90-7;MeOSuc-AAPV-PNA;MeOSuc-Ala-Ala-Pro-Val-PNA;MeOSuc-AAPV-pNA, Chromogenic Substrate;N-Methoxysuccinyl-Ala-Ala-Pro-Val p-nitroanilide;MeOSuc-Ala-Ala-Pro-Val-pNA;;MFCD00077137;Meo-Suc-Ala-Ala-Pro-Val-Paranitroanilide;VLVGCNNWNUERRZ-OSAZLGQLSA-N;HY-P2685;AKOS037643618;AKOS040756389;AS-17783;DA-55341;FM110732;methyl 3-{[(1S)-1-{[(2S)-1-[(2S)-2-{[(1S)-2-methyl-1-[(4-nitrophenyl)carbamoyl]propyl]carbamoyl}pyrrolidin-1-yl]-1-oxopropan-2-yl]carbamoyl}ethyl]carbamoyl}propanoate;CS-0139184;G77869;N-methoxysuccinyl-ala-ala-pro-val-p-nitroanilide;Elastase Substrate I, Colorimetric - CAS 70967-90-7;Methoxysuccinyl-Ala-Ala-Pro-Val-p-nitroanilide - CAS 70967-90-7;N-Methoxysuccinyl-Ala-Ala-Pro-Val p-nitroanilide, elastase substrate;methyl 4-((S)-1-((S)-1-((S)-2-((S)-3-methyl-1-(4-nitrophenylamino)-1-oxobutan-2-ylcarbamoyl)pyrrolidin-1-yl)-1-oxopropan-2-ylamino)-1-oxopropan-2-ylamino)-4-oxobutanoate;
N-Methoxysuccinyl-Ala-Ala-Pro-Val p-nitroanilide is a synthetic peptide substrate widely recognized for its role in biochemical research, particularly in the study of protease activity. Structurally, it features a sequence of amino acids capped with an N-methoxysuccinyl group at the N-terminus and a p-nitroanilide moiety at the C-terminus, which serves as a chromogenic leaving group. This configuration makes the compound highly suitable for enzymatic assays, allowing for sensitive detection of proteolytic cleavage events. Its design is tailored for specificity toward certain serine proteases, enabling researchers to investigate enzyme kinetics, substrate specificity, and regulatory mechanisms within complex biological systems.
Enzyme Activity Assays: The substrate is extensively employed in quantitative assays to measure the activity of serine proteases, such as elastase and related enzymes. Upon enzymatic cleavage at the peptide bond adjacent to the p-nitroanilide group, a colored p-nitroaniline product is released, which can be monitored spectrophotometrically. This chromogenic response offers a reliable and straightforward method for assessing enzyme kinetics, inhibitor efficacy, and substrate specificity, making it indispensable in protease characterization studies.
Inhibitor Screening: The compound plays a pivotal role in drug discovery and biochemical research focused on identifying and characterizing protease inhibitors. By incorporating the substrate into high-throughput screening platforms, researchers can rapidly evaluate the potency and selectivity of candidate compounds. The clear spectrophotometric readout enables precise determination of inhibitory concentrations and mechanistic insights into inhibitor-enzyme interactions, thereby facilitating the development of novel modulators of protease activity.
Substrate Specificity Profiling: N-Methoxysuccinyl-Ala-Ala-Pro-Val p-nitroanilide is frequently utilized to probe the substrate preferences of various proteases. Its defined peptide sequence allows for systematic investigation of enzyme-substrate recognition, elucidating the structural determinants that govern catalytic efficiency and selectivity. Such profiling is vital for mapping protease function in physiological and pathological contexts, as well as for guiding the rational design of improved substrates or inhibitors.
Biochemical Pathway Analysis: Researchers employ this substrate in studies aimed at dissecting proteolytic pathways within cellular and tissue extracts. By monitoring the cleavage of the peptide under different experimental conditions, it is possible to track dynamic changes in protease activity, assess the impact of regulatory factors, and uncover novel roles for proteolytic enzymes in signal transduction, protein turnover, or extracellular matrix remodeling.
Analytical Method Development: The chromogenic properties and well-defined cleavage kinetics of the substrate make it a valuable tool in the development and validation of analytical methods for protease quantification. Laboratories utilize it to calibrate assay systems, establish standard curves, and ensure reproducibility across experimental workflows. Its consistent performance underpins the reliability of protease assays in both academic and industrial research settings, supporting advancements in enzymology, diagnostics, and bioprocess monitoring.
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