N-Succinyl-Ala-Ala-Val p-nitroanilide serves as a chromogenic substrate with a tripeptide core tailored for protease-mapping assays. The nitroaniline reporter enables rapid spectroscopic detection of cleavage events. Researchers apply it to evaluate catalytic specificity and inhibitor behavior. Its succinyl group enhances aqueous compatibility.
CAT No: R2248
CAS No:61043-47-8
Synonyms/Alias:N-Succinyl-Ala-Ala-Val p-nitroanilide;Suc-Ala-Ala-Val-pNA;61043-47-8;MFCD00038473;IFAOJWCXOQHSQT-LXIYXOSZSA-N;FS110738;NS00054211;4-((S)-1-((S)-1-((S)-3-methyl-1-(4-nitrophenylamino)-1-oxobutan-2-ylamino)-1-oxopropan-2-ylamino)-1-oxopropan-2-ylamino)-4-oxobutanoic acid;4-[[(2S)-1-[[(2S)-1-[[(2S)-3-methyl-1-(4-nitroanilino)-1-oxobutan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid;
N-Succinyl-Ala-Ala-Val p-nitroanilide, also known as Suc-Ala-Ala-Val-pNA, is a synthetic chromogenic substrate widely utilized in biochemical and enzymological research. This peptide derivative incorporates a p-nitroanilide (pNA) group at its C-terminus, enabling sensitive colorimetric detection of enzymatic activity. The N-succinyl modification not only enhances the substrate's solubility and stability but also provides selectivity for specific proteases, making it an invaluable tool for researchers investigating proteolytic mechanisms. Its unique sequence and structural features render it particularly suitable for in vitro studies, high-throughput screening, and detailed kinetic analyses, supporting the advancement of fundamental and applied biosciences.
Protease Activity Assays: N-Succinyl-Ala-Ala-Val p-nitroanilide serves as a preferred substrate for quantifying the activity of serine proteases, especially those with chymotrypsin-like specificity. Upon enzymatic cleavage, the p-nitroanilide moiety is released, producing a yellow chromophore that can be quantitatively measured by absorbance at 405 nm. This property facilitates rapid, sensitive, and reproducible assessment of protease function in complex biological mixtures or purified systems, enabling researchers to monitor enzyme kinetics, inhibitor potency, and substrate specificity with precision.
Enzyme Characterization and Kinetics: Suc-Ala-Ala-Val-pNA is instrumental in detailed kinetic studies of proteolytic enzymes. By providing a defined and consistent substrate, it allows for the determination of key parameters such as Km and Vmax, as well as the elucidation of catalytic mechanisms. Researchers can systematically vary substrate concentrations and reaction conditions to dissect enzyme behavior, compare mutant or engineered proteases, and explore structure-activity relationships, thereby contributing to a deeper understanding of enzyme function at the molecular level.
High-Throughput Screening: The chromogenic nature of this peptide substrate makes it highly amenable to automated high-throughput screening (HTS) platforms. Laboratories engaged in drug discovery or inhibitor development often employ Suc-Ala-Ala-Val-pNA in microplate-based assays to rapidly evaluate large compound libraries for modulators of protease activity. The straightforward colorimetric readout streamlines data acquisition and analysis, accelerating the identification of promising candidate molecules for further investigation.
Biochemical Pathway Analysis: In studies focused on proteolytic pathways, N-Succinyl-Ala-Ala-Val p-nitroanilide enables researchers to dissect the roles of specific enzymes within complex cascades. By selectively monitoring the cleavage of this substrate in cell lysates, tissue extracts, or reconstituted systems, scientists can map protease activity profiles, investigate regulatory mechanisms, and assess the impact of genetic or pharmacological interventions on proteolytic processing. This targeted approach supports the elucidation of physiological and pathological processes involving protease function.
Quality Control and Enzyme Manufacturing: The substrate is also employed in quality control protocols during the production and purification of proteolytic enzymes. Manufacturers and researchers utilize Suc-Ala-Ala-Val-pNA to verify enzyme activity, lot-to-lot consistency, and stability over time. This application ensures that enzyme preparations meet required performance criteria for downstream research or industrial applications, supporting reliable and reproducible results across diverse experimental workflows.
Peptide substrate N-Succinyl-Ala-Ala-Val p-nitroanilide continues to be an essential reagent in enzymology, biotechnology, and molecular biology. Its versatility as a chromogenic substrate enables precise quantification and characterization of protease activity, supports the development of novel inhibitors, and facilitates the dissection of complex biochemical pathways. By providing a sensitive, reliable, and easy-to-use tool for enzyme analysis, it advances scientific discovery and innovation in both academic and industrial settings, underscoring its enduring value to the research community.
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