N-Cbz-Gly-Pro-Arg p-Nitroanilide Acetate Salt combines a protected tripeptide with a chromogenic reporter to measure enzymatic activity. Gly-Pro supports turn formation, while arginine enhances substrate affinity through electrostatic interactions. Researchers monitor p-nitroaniline release for kinetic evaluation. Uses include protease screening, catalytic-mechanism studies, and substrate validation.
CAT No: R2495
CAS No:102679-70-9
Synonyms/Alias:102679-70-9;N-Cbz-Gly-Pro-Arg p-nitro-anilide acetate salt;acetic acid;benzyl N-[2-[(2S)-2-[[(2S)-5-(diaminomethylideneamino)-1-(4-nitroanilino)-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-2-oxoethyl]carbamate;Z-Gly-Pro-Arg-pNA acetate;DTXSID20745562;MFCD18782526;NS00064810;Z-Gly-Pro-Arg p-nitroanilide acetate salt, protease substrate;Acetic acid--N-[(benzyloxy)carbonyl]glycyl-L-prolyl-N~5~-(diaminomethylidene)-N-(4-nitrophenyl)-L-ornithinamide (1/1);benzyl 2-((S)-2-((S)-5-guanidino-1-(4-nitrophenylamino)-1-oxopentan-2-ylcarbamoyl)pyrrolidin-1-yl)-2-oxoethylcarbamate acetate;
N-Cbz-Gly-Pro-Arg p-nitro-anilide acetate salt is a synthetic peptide substrate widely recognized for its utility in biochemical research, particularly in the study of protease activity and specificity. Structurally, it incorporates a carbobenzoxy (Cbz) protecting group at the N-terminus, a Gly-Pro-Arg tripeptide sequence, and a p-nitroanilide (pNA) chromogenic reporter, formulated as the acetate salt for enhanced solubility and stability. This compound plays a significant role in enzymology, enabling precise kinetic and mechanistic studies of proteolytic enzymes, especially those with trypsin-like specificity. Its design allows for sensitive detection and quantification of enzymatic cleavage events, making it a valuable tool in both academic and industrial research settings.
Enzyme substrate assays: As a chromogenic peptide substrate, N-Cbz-Gly-Pro-Arg p-nitro-anilide acetate salt is extensively employed in the quantitative assessment of serine protease activity, particularly enzymes such as trypsin, thrombin, and related proteases. Upon enzymatic cleavage at the arginine residue, the p-nitroanilide moiety is released, producing a measurable colorimetric change that can be detected spectrophotometrically. This enables researchers to monitor enzyme kinetics in real time, facilitating the determination of catalytic parameters such as Km and Vmax, and supporting detailed characterization of protease function.
Protease inhibitor screening: The substrate is instrumental in high-throughput screening protocols aimed at identifying and characterizing inhibitors of serine proteases. By providing a reliable and quantifiable readout of proteolytic activity, it allows for the rapid evaluation of potential inhibitory compounds and the assessment of their potency. This application is particularly valuable in early-stage drug discovery and in the investigation of regulatory mechanisms governing protease function in various biological systems.
Enzyme specificity profiling: Researchers utilize N-Cbz-Gly-Pro-Arg p-nitro-anilide acetate salt to elucidate the substrate specificity of proteolytic enzymes, especially those with arginine or trypsin-like preferences. By comparing the rate and extent of substrate hydrolysis across different enzymes or enzyme mutants, it becomes possible to map active site preferences, define substrate recognition motifs, and guide rational enzyme engineering efforts. Such specificity studies are crucial for both fundamental enzymology and the development of tailored biocatalysts.
Quality control in enzyme production: In industrial and biotechnological contexts, the compound serves as a standard substrate for the quality control of protease preparations. Routine activity assays using this chromogenic peptide enable manufacturers to verify enzyme potency, monitor batch-to-batch consistency, and ensure the reliability of protease products destined for downstream applications. The reproducibility and sensitivity of the colorimetric assay support robust process validation and product release testing.
Educational and methodological development: Owing to its well-defined cleavage mechanism and straightforward assay readout, the substrate is frequently incorporated into laboratory teaching modules and methodological development projects. It provides a practical and illustrative example for demonstrating the principles of enzyme kinetics, substrate turnover, and spectrophotometric analysis, making it a preferred choice for both instructional and protocol optimization purposes. Its versatility in assay design further supports the advancement of novel analytical techniques in protease research.
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