N-p-Tosyl-Gly-Pro-Lys-pNA is a colorimetric substrate for plasmin. Plasmin binds and hydrolyzes N-p-tosyl-Gly-Pro-Lys-pNA to release p-nitroanilide (pNA), which can be quantified by colorimetric detection at 405 nm as a measure of plasmin activity.
CAT No: R1907
CAS No:88793-79-7
Synonyms/Alias:88793-79-7;N-p-Tosyl-Gly-Pro-Lys p-nitroanilide acetate salt;N-(p-Tosyl)-Gly-Pro-Lys 4-nitroanilide acetate salt;acetic acid;(2S)-N-[(2S)-6-amino-1-(4-nitroanilino)-1-oxohexan-2-yl]-1-[2-[(4-methylphenyl)sulfonylamino]acetyl]pyrrolidine-2-carboxamide;N-p-Tosyl-Gly-Pro-Lys-pNA (acetate);Tos-GPK-pNA;Tos-Gly-Pro-Lys-pNA acetate;MFCD00057232;SCHEMBL16234756;KPGSNEYSJPIZCW-SJEIDVEUSA-N;AKOS040755132;HY-137798;CS-0142060;N-p-tosyl-gly-pro-lysp-nitroanilideacetatesalt;N-(p-tosyl)-gly-pro-lys-4 nitroanilide acetate salt;N-(p-Tosyl)-Gly-Pro-Lys 4-nitroanilide acetate salt, plasmin substrate;(S)-N-((S)-6-amino-1-(4-nitrophenylamino)-1-oxohexan-2-yl)-1-(2-(4-methylphenylsulfonamido)acetyl)pyrrolidine-2-carboxamide acetate;
Chemical Name:N-[(4-methylphenyl)sulfonyl]glycyl-L-prolyl-N-(4-nitrophenyl)-L-lysinamide, monoacetate
N-p-Tosyl-Gly-Pro-Lys p-nitroanilide acetate salt is a synthetic peptide substrate widely recognized for its utility in protease research and enzymology. As a chromogenic tripeptide incorporating a p-nitroanilide (pNA) group at the C-terminus, this compound is engineered to facilitate sensitive detection of enzymatic cleavage events. The presence of the N-p-tosyl group confers enhanced stability and specificity, while the acetate salt form aids in solubility and handling. Its well-defined sequence and chromophoric properties make it particularly valuable in studies focused on proteolytic enzyme activity, substrate specificity, and inhibitor screening, providing a robust tool for both basic and applied biochemical investigations.
Enzyme kinetics: Utilization of this peptide substrate is central in quantitative assays designed to measure serine protease activity, especially those with trypsin-like specificity. Upon proteolytic cleavage at the lysine residue, the p-nitroanilide moiety is released, producing a distinct yellow color measurable spectrophotometrically. This chromogenic response enables precise determination of reaction rates, Michaelis-Menten parameters, and kinetic constants, supporting detailed mechanistic studies and comparative analyses of enzyme variants.
Substrate specificity profiling: The defined sequence of Gly-Pro-Lys within the molecule allows researchers to systematically evaluate the substrate preferences of various proteases. By monitoring the rate and extent of pNA release, scientists can delineate the substrate recognition motifs of target enzymes, map active site interactions, and refine understanding of enzyme-substrate complementarity. Such insights are crucial for enzyme engineering, functional annotation, and the rational design of novel substrates.
Inhibitor screening: The chromogenic properties of the p-nitroanilide group make this peptide an effective tool for high-throughput screening of protease inhibitors. Inhibition assays utilizing this substrate enable rapid assessment of compound efficacy by quantifying decreases in color development, offering a straightforward and reproducible method for evaluating potential drug candidates, lead compounds, or molecular probes in enzymatic systems.
Quality control and validation: Biopharmaceutical and enzyme production processes often require rigorous quality control measures to ensure product consistency and activity. This chromogenic peptide substrate serves as a reliable reagent for validating the functional integrity of protease preparations, confirming lot-to-lot consistency, and monitoring the stability of enzyme formulations over time. Its use in standardized assays supports compliance with internal research protocols and industry best practices.
Biochemical assay development: The versatility and sensitivity of this substrate facilitate its integration into a wide range of custom assay platforms. It can be adapted for use in microplate formats, automated liquid handling systems, or continuous monitoring setups, allowing researchers to tailor experimental conditions to specific research objectives. Its robust performance under various buffer systems and conditions further enhances its suitability for optimizing assay sensitivity, throughput, and reproducibility in both academic and industrial laboratories.
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