Meosuc-aapm-pna is a chromogenic peptide substrate containing an activated nitroanilide group for monitoring proteolytic cleavage. The sequence architecture provides well-defined recognition elements for mapping enzyme specificity. Researchers employ it for kinetic profiling and structure-function studies. Its ester-linked protecting groups enhance solubility and stability in assay systems.
CAT No: R2252
CAS No:70967-91-8
Synonyms/Alias:MEOSUC-AAPM-PNA;70967-91-8;methyl 4-[[1-[[1-[2-[[4-methylsulfanyl-1-(4-nitroanilino)-1-oxobutan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoate;N-Methoxysuccinyl-Ala-Ala-Pro-Met p-nitroanilide;CATHEPSIN G SUBSTRATE;DTXSID20404147;VCA96791;AS-87836;G77868;N-Methoxysuccinyl-Ala-Ala-Pro-Met p-nitroanilide, >95% (HPLC);
Meosuc-aapm-pna is a synthetic peptide compound designed for advanced biochemical research and peptide-based investigations. Characterized by its defined amino acid sequence and specialized protecting groups, this molecule is tailored for applications in protease substrate studies, enzymatic activity assays, and peptide synthesis methodologies. Its structural features, including the presence of a methoxy succinyl (Meosuc) group and a para-nitroanilide (pNA) moiety, make it highly valuable for monitoring proteolytic cleavage events and facilitating quantitative analysis in enzymology. As a research-use peptide substrate, Meosuc-aapm-pna is integral to the development and optimization of biochemical assays that probe protease specificity, mechanism, and inhibition.
Enzyme Substrate Assays: In the context of protease research, Meosuc-aapm-pna is widely utilized as a chromogenic substrate for serine proteases, particularly those with specificity for the AAPM sequence. Upon enzymatic cleavage, the release of the para-nitroanilide group generates a measurable colorimetric signal, enabling real-time quantification of proteolytic activity. This functional property supports the development of sensitive, high-throughput assays for characterizing enzyme kinetics, substrate specificity, and catalytic efficiency in both basic and applied research settings.
Inhibitor Screening: The compound's well-defined cleavage site and chromogenic readout make it an excellent tool for screening and evaluating potential protease inhibitors. By incorporating this substrate into inhibition assays, researchers can rapidly assess the efficacy and selectivity of small molecules, peptides, or biological extracts in modulating target enzyme activity. The quantitative output provided by the pNA release facilitates detailed structure-activity relationship studies and aids in the identification of novel inhibitory compounds.
Peptide Synthesis Validation: As a model substrate, Meosuc-aapm-pna serves an important role in validating solid-phase peptide synthesis protocols and post-synthetic modifications. Its sequence and protecting groups allow researchers to assess coupling efficiency, deprotection strategies, and overall product integrity during method development. The ability to monitor cleavage of this substrate by specific proteases also provides a functional readout for confirming the correct assembly and biological relevance of synthesized peptides.
Mechanistic Enzymology: The structural design of Meosuc-aapm-pna supports in-depth mechanistic studies of proteolytic enzymes. By analyzing cleavage patterns and reaction kinetics with this substrate, investigators can elucidate enzyme-substrate interactions, transition state stabilization, and the influence of active site residues on catalysis. Such mechanistic insights are critical for advancing the understanding of protease function in physiological and pathological contexts, as well as for informing rational enzyme engineering efforts.
Analytical Method Development: The chromogenic properties of Meosuc-aapm-pna enable its use in the development and optimization of analytical methods for protease detection and quantification. Its consistent and reproducible response to enzymatic cleavage makes it suitable for calibration, method validation, and comparative studies across different assay platforms. This utility extends to the quality control of enzyme preparations and the standardization of proteolytic assays in research laboratories and biotechnology workflows.
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