MeoSuc-Ala-Ala-Pro-Val-AMC

MeOSuc-AAPV-AMC is a fluorogenic substrate for human leukocyte and porcine pancreatic elastase.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: 10-101-307

CAS No:72252-90-5

Synonyms/Alias:MeOSuc-Ala-Ala-Pro-Val-7-Amino-4-Methylcoumarin; MeOSuc-AAPV-AMC

Chemical Name:methyl 4-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S)-3-methyl-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxobutan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoate

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M.F/Formula
C31H41N5O9
M.W/Mr.
627.7
Sequence
One Letter Code: MeOSuc-AAPV-AMC
Three Letter Code: MeOSuc-Ala-Ala-Pro-Val-AMC
Appearance
White to off-white powder
Purity
≥95% (HPLC)

MeoSuc-Ala-Ala-Pro-Val-AMC, also known as Methoxysuccinyl-Ala-Ala-Pro-Val-7-amido-4-methylcoumarin, is a synthetic peptide substrate widely utilized in biochemical and molecular biology research. Characterized by its unique sequence and the AMC (7-amido-4-methylcoumarin) fluorogenic leaving group, this compound serves as a powerful tool for monitoring enzyme activity, particularly serine proteases such as neutrophil elastase. Its design enables sensitive detection of enzymatic cleavage events, making it highly valuable in both basic and applied research contexts. The incorporation of the methoxysuccinyl group enhances substrate specificity, while the peptide sequence mimics physiological substrates, facilitating accurate assessment of protease function. The fluorogenic AMC moiety, upon enzymatic hydrolysis, releases a fluorescent signal, allowing for real-time and quantitative analysis of proteolytic activity in various experimental systems.

Enzyme Kinetics Assays: In enzyme kinetics studies, MeoSuc-Ala-Ala-Pro-Val-AMC is extensively employed to characterize the activity of serine proteases, especially neutrophil elastase. Researchers utilize this substrate to determine kinetic parameters such as Km and Vmax by measuring the rate of AMC release under different substrate concentrations. Its high sensitivity and specificity enable precise quantification of enzyme activity, facilitating the investigation of enzyme mechanisms, substrate preferences, and the effects of mutations or inhibitors on catalytic efficiency. This substrate supports both endpoint and continuous assay formats, making it adaptable to various experimental designs and throughput requirements.

Inhibitor Screening: Methoxysuccinyl-Ala-Ala-Pro-Val-AMC plays a critical role in the screening and characterization of protease inhibitors. By providing a reliable and sensitive readout of protease activity, it allows researchers to evaluate the efficacy and selectivity of potential inhibitory compounds. The fluorogenic nature of the substrate ensures that even low levels of enzymatic inhibition can be detected, supporting the identification of lead compounds for further development. Its compatibility with high-throughput screening platforms accelerates the drug discovery process in projects targeting serine proteases implicated in diverse pathological processes.

Protease Profiling: The substrate is an essential component in protease profiling studies, where researchers aim to differentiate between various protease activities present in complex biological samples. By employing MeoSuc-Ala-Ala-Pro-Val-AMC in multiplexed or comparative assays, scientists can distinguish neutrophil elastase activity from other proteases based on substrate specificity and cleavage efficiency. This capability is valuable for deciphering the proteolytic landscape in physiological and pathological conditions, aiding in the identification of biomarkers or therapeutic targets.

Cellular and Tissue Extract Studies: In studies involving cellular lysates or tissue extracts, the fluorogenic substrate enables the direct measurement of protease activity in biologically relevant environments. Researchers can monitor changes in enzyme activity in response to stimuli, disease states, or genetic modifications, gaining insights into regulatory mechanisms and functional consequences. The substrate's stability and low background fluorescence ensure reliable results in complex sample matrices, supporting translational research and systems biology investigations.

Biochemical Method Development: Methoxysuccinyl-Ala-Ala-Pro-Val-AMC is frequently utilized in the development and optimization of novel biochemical assays for protease detection and quantification. Its predictable cleavage and robust fluorescence response make it a preferred choice for establishing standardized protocols in academic, pharmaceutical, and biotechnology laboratories. The substrate facilitates the validation of new assay formats, contributes to the refinement of analytical workflows, and supports the implementation of automated or miniaturized screening systems for protease research.

High-Content Screening: In addition to its applications in enzyme kinetics and inhibitor discovery, MeoSuc-Ala-Ala-Pro-Val-AMC is valuable in high-content screening approaches where multiple parameters are assessed simultaneously. Researchers leverage its fluorogenic properties to monitor protease activity in conjunction with other cellular events, enabling comprehensive phenotypic analyses. The substrate's compatibility with multiwell plate formats and automated imaging platforms enhances experimental throughput and data richness, driving innovation in protease-targeted research and compound evaluation.

Long-term Storage Conditions
ethanol: 1 mg/mL
DMF: 5 mg/mL
DMSO: 5 mg/Ml
Shipping Condition
+20°C (International: -20°C)
InChI
InChI=1S/C31H41N5O9/c1-16(2)27(30(42)34-20-9-10-21-17(3)14-26(39)45-23(21)15-20)35-29(41)22-8-7-13-36(22)31(43)19(5)33-28(40)18(4)32-24(37)11-12-25(38)44-6/h9-10,14-16,18-19,22,27H,7-8,11-13H2,1-6H3,(H,32,37)(H,33,40)(H,34,42)(H,35,41)/t18-,19-,22-,27-/m0/s1
InChI Key
CMEUDEVBFFPSEI-NFHWZJRKSA-N
Canonical SMILES
CC1=CC(=O)OC2=C1C=CC(=C2)NC(=O)C(C(C)C)NC(=O)C3CCCN3C(=O)C(C)NC(=O)C(C)NC(=O)CCC(=O)OC
Isomeric SMILES
CC1=CC(=O)OC2=C1C=CC(=C2)NC(=O)[C@H](C(C)C)NC(=O)[C@@H]3CCCN3C(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)CCC(=O)OC

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