MeOSuc-AAPV-AFC integrates a methoxysuccinyl-protected peptide sequence with a fluorogenic AFC group for monitoring enzymatic cleavage. Residue selection supports protease-recognition studies and kinetic profiling. Researchers assess fluorescence changes to characterize catalytic behavior. Uses include substrate-validation assays, enzyme-mechanism mapping, and biochemical method development.
CAT No: R2338
CAS No:125791-90-4
Synonyms/Alias:MeOSuc-AAPV-AFC;Meosuc-Ala-Ala-Pro-Val-7-Amino-4-Trifluoro-Methylcoumarin;FLFLPZJVJVKNIW-BYRWETQCSA-N;HY-P5374;DA-55339;CS-0882855;125791-90-4;methyl 4-((S)-1-((S)-1-((S)-2-((S)-3-methyl-1-oxo-1-(2-oxo-4-(trifluoromethyl)-2H-chromen-7-ylamino)butan-2-ylcarbamoyl)pyrrolidin-1-yl)-1-oxopropan-2-ylamino)-1-oxopropan-2-ylamino)-4-oxobutanoate;
MeOSuc-AAPV-AFC is a synthetic peptide substrate featuring a methoxysuccinyl (MeOSuc) blocking group, a defined tetrapeptide sequence (Ala-Ala-Pro-Val), and a 7-amino-4-trifluoromethylcoumarin (AFC) fluorogenic reporter. As a biochemically engineered peptide compound, it is widely recognized for its utility in enzymatic assays targeting serine proteases, particularly neutrophil elastase. The design of this substrate enables sensitive and specific detection of proteolytic activity through fluorescence-based readouts, making it a valuable tool in protease research, inhibitor screening, and mechanistic enzymology. Its structure and functional attributes facilitate precise monitoring of enzyme-substrate interactions, supporting a range of investigative and high-throughput applications in modern biochemical research.
Enzyme Activity Assays: MeOSuc-AAPV-AFC is extensively used in the quantitative assessment of serine protease activity, especially neutrophil elastase. Upon enzymatic cleavage at the peptide bond, the AFC moiety is released, resulting in a measurable fluorescent signal. This property allows for real-time kinetic analysis of protease activity in complex biological samples or purified systems, providing researchers with a robust platform for characterizing enzyme specificity, catalytic efficiency, and substrate preferences.
Inhibitor Screening: The fluorogenic nature of this peptide substrate makes it an ideal choice for high-throughput screening of protease inhibitors. By monitoring changes in fluorescence in the presence of candidate compounds, researchers can efficiently evaluate the potency and selectivity of small molecule or peptide-based inhibitors. This approach is instrumental in early-stage drug discovery and the development of novel chemical probes targeting serine proteases.
Mechanistic Enzymology: The defined sequence and modular design of MeOSuc-AAPV-AFC support detailed mechanistic studies of protease function. Researchers leverage this substrate to dissect substrate recognition motifs, investigate active site dynamics, and elucidate catalytic mechanisms. The ability to monitor substrate turnover in real time enhances the resolution of mechanistic insights, facilitating the design of more effective enzyme modulators and synthetic substrates.
Protease Profiling: In complex biological matrices, such as cell lysates or tissue extracts, the substrate serves as a selective probe for profiling serine protease activity. Its specificity for elastase-like enzymes enables differential analysis of protease expression, regulation, and activity under various physiological or pathological conditions. This application is valuable for biomarker discovery, basic research, and comparative studies across different sample types.
Assay Development and Optimization: The reliable fluorescence response and well-characterized cleavage site of MeOSuc-AAPV-AFC make it a preferred standard in the development and optimization of protease assays. Researchers utilize it to calibrate assay sensitivity, determine optimal substrate concentrations, and validate assay performance parameters. Its consistent behavior across diverse assay platforms ensures reproducibility and comparability of experimental results, supporting rigorous methodological standards in protease research.
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