Z-Leu-Arg-7-Amino-4-Methylcoumarin links a protected dipeptide to a fluorogenic AMC reporter, enabling sensitive protease-detection assays. Leucine and arginine define hydrophobic and basic recognition features. Researchers analyze cleavage kinetics via fluorescence output. Uses include substrate profiling, enzyme screening, and mechanistic studies.
CAT No: R2479
CAS No:156192-32-4
Synonyms/Alias:156192-32-4;Z-Leu-Arg-7-Amino-4-Methylcoumarin;Z-Leu-Arg-AMC;benzyl N-[(2S)-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate;Z-Leu-Arg-Amc HCl;CBZ-Leu-Arg-AMC;CHEMBL126324;SCHEMBL5523268;BDBM12033;Cathepsin K Substrate (fluorogenic);MFCD07780911;FL110604;HY-142021;benzyloxycarbonyl-Leu-Arg-7-amino-4-methyl-coumarin;Benzyl ((S)-1-(((S)-5-guanidino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxopentan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)carbamate;benzyl (S)-1-((S)-5-guanidino-1-(4-methyl-2-oxo-2H-chromen-7-ylamino)-1-oxopentan-2-ylamino)-4-methyl-1-oxopentan-2-ylcarbamate;benzyl N-[(1S)-1-{[(1S)-4-carbamimidamido-1-[(4-methyl-2-oxo-2H-chromen-7-yl)carbamoyl]butyl]carbamoyl}-3-methylbutyl]carbamate;benzyl N-[(1S)-1-{[(1S)-4-carbamimidamido-1-[(4-methyl-2-oxochromen-7-yl)carbamoyl]butyl]carbamoyl}-3-methylbutyl]carbamate;
Z-Leu-Arg-7-Amino-4-Methylcoumarin is a synthetic peptide substrate featuring a coumarin-based fluorogenic leaving group. As a conjugate of the dipeptide Z-Leucine-Arginine and the fluorescent moiety 7-amino-4-methylcoumarin (AMC), this compound is widely recognized for its utility in enzymology and protease research. Its design enables precise monitoring of proteolytic activity, especially for serine and cysteine proteases with a preference for arginine at the P1 position. The robust fluorescence signal generated upon enzymatic cleavage makes it a valuable analytical tool for both qualitative and quantitative studies in biochemical research.
Enzyme Activity Assays: Z-Leu-Arg-7-Amino-4-Methylcoumarin is extensively employed as a fluorogenic substrate in the measurement of protease activity, particularly for trypsin-like and related serine proteases. Upon enzymatic hydrolysis at the peptide bond adjacent to arginine, the AMC group is released, resulting in a strong fluorescent signal that can be quantitatively measured. This property facilitates the development of sensitive, high-throughput assays for enzyme kinetics, inhibitor screening, and mechanistic studies.
Protease Specificity Profiling: The dipeptide sequence incorporated into this substrate allows researchers to probe the substrate specificity of various proteolytic enzymes. By comparing the cleavage efficiency of Z-Leu-Arg-AMC with other peptide-AMC substrates, scientists can delineate the substrate preferences of target proteases. This approach supports the rational design of selective inhibitors and contributes to the functional characterization of novel or engineered proteolytic enzymes.
Drug Discovery and Screening: In the context of early-phase drug discovery, the compound serves as a reliable reporter in high-throughput screening platforms for protease inhibitors. The robust and reproducible fluorescence generated upon substrate cleavage enables rapid assessment of compound libraries for inhibitory activity, supporting lead identification and optimization efforts in pharmaceutical research targeting proteolytic pathways.
Biochemical Pathway Analysis: The use of this fluorogenic peptide substrate extends to the elucidation of protease function within complex biological samples, such as cell lysates or tissue extracts. By enabling real-time detection of enzyme activity, it aids in mapping proteolytic events, monitoring changes in protease expression, and studying regulatory mechanisms under various physiological and experimental conditions.
Enzyme Kinetics and Mechanistic Studies: The sensitivity and quantitative nature of the fluorescence readout provided by Z-Leu-Arg-7-Amino-4-Methylcoumarin make it ideal for detailed kinetic analyses. Researchers can determine critical parameters such as Km and Vmax, investigate enzyme-substrate interactions, and explore the effects of mutations or post-translational modifications on proteolytic efficiency. These insights are crucial for advancing the understanding of enzyme mechanisms and for the rational engineering of proteolytic enzymes for research or industrial applications.
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