N-Methoxysuccinyl-Ala-Ala-Pro-Val

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.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
N-Methoxysuccinyl-Ala-Ala-Pro-Val(CAS 107441-48-5)

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;

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M.F/Formula
C21H34N4O8
M.W/Mr.
470.5
Sequence
One Letter Code:AAPV
Three Letter Code:MeOSuc-DL-Ala-DL-Ala-DL-Pro-DL-Val-OH

N-Methoxysuccinyl-Ala-Ala-Pro-Val is a synthetic peptide substrate widely recognized for its utility in enzymology and biochemical research. Characterized by its unique sequence and the presence of a methoxysuccinyl group, this compound offers enhanced stability and specificity in experimental assays. Its structure is specifically designed to interact with certain proteolytic enzymes, making it an indispensable tool for probing enzyme activity and substrate specificity. The versatility of N-Methoxysuccinyl-Ala-Ala-Pro-Val has led to its adoption in various scientific disciplines, where precision and reproducibility are critical for advancing knowledge of protease function and regulation.

Enzyme Activity Assays: N-Methoxysuccinyl-Ala-Ala-Pro-Val is extensively utilized as a chromogenic or fluorogenic substrate in enzyme activity assays, particularly for serine proteases such as elastase. Researchers employ this peptide to quantitatively measure proteolytic activity by monitoring the release of chromophores or fluorophores upon enzymatic cleavage. The substrate's sequence is optimized for selective recognition, enabling accurate kinetic studies and inhibitor screening in both basic research and pharmaceutical development. The use of this substrate simplifies the assessment of enzyme function and facilitates the identification of modulators with potential therapeutic relevance.

Protease Specificity Profiling: In studies aiming to elucidate the substrate specificity of various proteases, N-Methoxysuccinyl-Ala-Ala-Pro-Val serves as a model peptide. Its defined sequence allows scientists to systematically investigate how different enzymes interact with peptide bonds, shedding light on catalytic preferences and mechanisms. By comparing the cleavage efficiency of this substrate across different protease families, researchers can draw meaningful conclusions about enzyme-substrate interactions and the structural determinants underlying specificity. This information is invaluable for the rational design of selective inhibitors and for understanding physiological proteolytic processes.

High-Throughput Screening: The application of N-Methoxysuccinyl-Ala-Ala-Pro-Val in high-throughput screening platforms streamlines the discovery of novel protease inhibitors and activators. Its compatibility with automated assay systems enables rapid and reproducible testing of large compound libraries, accelerating the pace of drug discovery and functional genomics research. The substrate's robust signal generation and low background interference make it particularly suitable for screening campaigns where sensitivity and reliability are paramount. By facilitating the identification of bioactive molecules, it supports the development of new therapeutic strategies targeting proteolytic enzymes.

Biochemical Pathway Analysis: Researchers leverage N-Methoxysuccinyl-Ala-Ala-Pro-Val to dissect complex biochemical pathways involving proteolytic processing. By integrating this substrate into in vitro and ex vivo models, scientists can monitor the activity of specific proteases under physiological or pathological conditions. This approach aids in mapping the roles of proteases in diverse biological processes, such as inflammation, tissue remodeling, and signal transduction. The insights gained from these studies contribute to a deeper understanding of cellular regulation and the molecular basis of disease progression.

Academic and Industrial Research: The widespread adoption of N-Methoxysuccinyl-Ala-Ala-Pro-Val in both academic and industrial laboratories underscores its value as a research tool. In academic settings, it supports fundamental investigations into enzyme mechanisms, structure-function relationships, and protein engineering. Industrial researchers utilize the peptide in the development and quality control of enzyme-based products, ensuring consistency and efficacy. Its reliability and well-characterized performance make it a preferred choice for studies requiring reproducible results and high analytical sensitivity. The collective body of research enabled by this substrate continues to advance the frontiers of protease biology and enzymology.

InChI
InChI=1S/C21H34N4O8/c1-11(2)17(21(31)32)24-19(29)14-7-6-10-25(14)20(30)13(4)23-18(28)12(3)22-15(26)8-9-16(27)33-5/h11-14,17H,6-10H2,1-5H3,(H,22,26)(H,23,28)(H,24,29)(H,31,32)
InChI Key
XSYKVGBBBLUSAQ-UHFFFAOYSA-N

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