MeO-Suc-Arg-Pro-Tyr-pNA is a substrate for Chymotrypsin.
CAT No: 10-101-347
Synonyms/Alias:N-Methoxy-Succinyl-L-Arginyl-L-Prolyl-L-Tyrosine-p-Nitroanilide
MeO-Suc-Arg-Pro-Tyr-pNA is a synthetic peptide substrate widely utilized in enzymology and biochemical research for its ability to facilitate precise measurement of protease activity. This compound features a sequence incorporating arginine, proline, and tyrosine residues, capped with a methoxy-succinyl (MeO-Suc) group at the N-terminus and a para-nitroanilide (pNA) moiety at the C-terminus. The presence of the pNA chromophore enables sensitive colorimetric detection upon enzymatic cleavage, making the substrate especially valuable in studies of serine proteases, including those with trypsin-like specificity. Its well-defined structure and reactivity have established it as a reliable tool for both fundamental research and assay development in the field of protein biochemistry.
Enzyme activity assays: Researchers frequently employ this peptide substrate in quantitative assays designed to monitor serine protease activity. Upon enzymatic hydrolysis at the peptide bond adjacent to the arginine residue, the pNA group is released, producing a distinct yellow color that can be measured spectrophotometrically. This approach allows for real-time monitoring of proteolytic reactions, enabling the determination of kinetic parameters such as Km and Vmax. The substrate's specificity and chromogenic properties make it highly suitable for high-throughput screening and detailed characterization of protease function in purified systems or complex biological samples.
Enzyme inhibitor screening: The chromogenic peptide is instrumental in the evaluation of potential protease inhibitors. By providing a clear and quantifiable readout of enzyme activity, it facilitates the assessment of compound efficacy in inhibiting target enzymes. Researchers can systematically test small molecules, peptides, or natural products for their ability to modulate serine protease activity, supporting drug discovery and mechanistic studies. The straightforward colorimetric detection of pNA release streamlines the process of comparing inhibition profiles across different candidate molecules.
Protease specificity profiling: Scientists utilize MeO-Suc-Arg-Pro-Tyr-pNA to investigate the substrate preferences and cleavage site selectivity of various serine proteases. By analyzing the rate and extent of substrate hydrolysis, insights can be gained into the structural determinants of enzyme-substrate recognition. This information is critical for mapping protease substrate specificity, guiding the rational design of selective inhibitors, and understanding the roles of these enzymes in physiological and pathological processes.
Analytical method development: The peptide substrate serves as a standard tool in the optimization and validation of analytical protocols for protease measurement. Laboratories developing novel assay platforms, including microplate-based or automated systems, rely on its consistent response and well-characterized cleavage kinetics. The substrate's robust performance supports the establishment of reproducible and sensitive methods for routine enzyme quantification, quality control, and research applications.
Biochemical pathway studies: In broader biochemical research, MeO-Suc-Arg-Pro-Tyr-pNA enables functional studies of protease-mediated processes within signaling cascades and regulatory networks. Its use in cell-free extracts or fractionated samples provides valuable information on endogenous protease activities, substrate processing, and the modulation of proteolytic events by physiological or experimental factors. The substrate's compatibility with diverse assay conditions supports its integration into studies of protein turnover, signal transduction, and enzymatic regulation in various biological systems.
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