N-Methoxysuccinyl-Ala-Ala-Pro-Val integrates a methoxysuccinyl protecting group that modulates recognition by enzymes. The proline residue introduces conformational constraints useful for mapping catalytic preferences. The sequence supports kinetic profiling and substrate-enzyme interaction studies. Research fields include protease specificity analysis, synthetic peptide development, and mechanistic enzymology.
CAT No: R2429
CAS No:107441-48-5
Synonyms/Alias:N-Methoxysuccinyl-Ala-Ala-Pro-Val;107441-48-5;MEOSUC-ALA-ALA-PRO-VAL-OH;2-[[1-[2-[2-[(4-methoxy-4-oxobutanoyl)amino]propanoylamino]propanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoic acid;DTXSID00401255;SCHEMBL25638189;DTXCID80352110;FM109085;
N-Methoxysuccinyl-Ala-Ala-Pro-Val is a synthetic peptide substrate widely recognized for its utility in biochemical and enzymological research. Structurally, it consists of a tetrapeptide sequence (Ala-Ala-Pro-Val) N-terminally modified with a methoxysuccinyl group, a modification that enhances its stability and specificity in various assay environments. The peptide is primarily valued for its role as a chromogenic or fluorogenic substrate in the study of protease activity, particularly for enzymes within the serine protease family such as neutrophil elastase and related proteolytic enzymes. Its defined sequence and chemical modification make it a reliable tool for dissecting enzyme-substrate specificity, kinetic properties, and inhibitor screening, all of which are crucial in both basic and applied biochemical research.
Protease activity assays: N-Methoxysuccinyl-Ala-Ala-Pro-Val is extensively employed as a substrate in protease activity assays, especially for characterizing the catalytic function of serine proteases like neutrophil elastase. The peptide's sequence is specifically recognized and cleaved by target enzymes, and the N-methoxysuccinyl group confers improved resistance to non-specific degradation, ensuring assay accuracy. Researchers utilize this substrate in spectrophotometric or fluorometric formats to quantitatively monitor enzymatic hydrolysis, enabling precise determination of enzyme kinetics, substrate affinity, and turnover rates. Such assays are foundational in understanding protease function in physiological and pathological contexts.
Enzyme inhibitor screening: The tetrapeptide substrate serves as a robust platform for screening and characterizing small molecule or peptide-based inhibitors of serine proteases. By providing a consistent and well-characterized cleavage site, N-Methoxysuccinyl-Ala-Ala-Pro-Val allows for the reliable assessment of inhibitor potency and specificity. Inhibitor studies using this substrate yield critical data on inhibition constants and mechanism of action, supporting the development of novel modulators for biochemical and pharmaceutical research. Its use in high-throughput screening protocols accelerates the identification of candidate molecules for further study.
Enzyme specificity profiling: The defined amino acid sequence and N-terminal modification of this substrate enable detailed investigations into the substrate specificity of various proteases. By comparing the cleavage efficiency of N-Methoxysuccinyl-Ala-Ala-Pro-Val with related peptide substrates, researchers can map the substrate preferences of enzymes, elucidate recognition motifs, and explore the structural determinants of proteolytic activity. Such profiling is instrumental in enzyme engineering, functional annotation of novel proteases, and the rational design of selective substrates or inhibitors.
Mechanistic enzymology: The substrate is frequently used in mechanistic studies aimed at elucidating the catalytic mechanisms of serine proteases. By varying substrate concentrations and analyzing reaction kinetics, scientists can dissect the steps involved in enzyme-substrate binding, catalysis, and product release. The stability and specificity of N-Methoxysuccinyl-Ala-Ala-Pro-Val facilitate reproducible experiments that yield high-quality kinetic data, contributing to a deeper understanding of enzyme function at the molecular level.
Analytical biochemistry: Beyond its direct use in enzymatic assays, the peptide substrate is valuable in analytical techniques that require sensitive detection of protease activity in complex biological samples. Its application extends to the quantification of enzyme activity in cell lysates, tissue extracts, and other biological matrices, supporting studies in cell biology, immunology, and disease research. The substrate's chemical characteristics enable selective detection and quantitation of target enzyme activity, making it an indispensable tool in modern biochemical analysis.
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