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, also known as Z-Leucyl-Arginyl-AMC or Z-Leu-Arg-AMC, is a synthetic peptide substrate widely recognized for its utility in enzymatic activity assays. Featuring a coumarin-based fluorogenic group, this compound enables sensitive detection of protease activity, specifically targeting enzymes that recognize the Leu-Arg sequence. The molecular structure incorporates a benzyloxycarbonyl (Z) protecting group, which enhances the stability of the peptide while preventing premature cleavage. Its unique design allows for real-time monitoring of enzymatic reactions through fluorescence emission upon substrate hydrolysis, making it a valuable tool in biochemical research. Researchers appreciate its compatibility with a variety of assay platforms, including microplate readers and fluorescence spectrophotometers, facilitating high-throughput screening and kinetic studies. Z-Leu-Arg-7-Amino-4-Methylcoumarin's versatility extends to applications in both fundamental and applied sciences, supporting advancements in enzymology, drug discovery, and molecular biology.
Protease Activity Assays: Z-Leu-Arg-7-Amino-4-Methylcoumarin serves as an essential substrate for the quantitative analysis of protease activity, particularly for trypsin-like serine proteases. Upon enzymatic cleavage at the Leu-Arg bond, the 7-amino-4-methylcoumarin moiety is released, producing a measurable fluorescent signal. This property allows for sensitive detection and kinetic characterization of proteases in complex biological samples or purified enzyme preparations. Its use streamlines the assessment of enzyme specificity, catalytic efficiency, and inhibitor profiling, supporting detailed mechanistic studies in protease research.
Enzyme Inhibitor Screening: Z-Leu-Arg-AMC is extensively employed in high-throughput screening assays to identify and evaluate potential protease inhibitors. By monitoring changes in fluorescence intensity in the presence of candidate compounds, researchers can rapidly assess inhibitory potency and selectivity. This approach accelerates the discovery of novel therapeutic agents targeting proteolytic enzymes, as well as the optimization of lead compounds. The substrate's robust fluorescence response enables precise quantification of enzyme inhibition, facilitating structure-activity relationship studies and guiding medicinal chemistry efforts.
Biochemical Pathway Analysis: In studies exploring proteolytic pathways, Z-Leucyl-Arginyl-AMC functions as a reliable probe for elucidating enzyme-substrate interactions and regulatory mechanisms. Researchers utilize its selective cleavage by specific proteases to dissect signaling cascades, post-translational modifications, and protein turnover processes. The ability to monitor real-time enzymatic reactions provides valuable insights into the dynamic regulation of proteolysis within cellular and subcellular contexts, advancing understanding of physiological and pathological processes.
Cellular and Molecular Biology Research: The fluorogenic properties of Z-Leu-Arg-7-Amino-4-Methylcoumarin make it a preferred substrate for investigating protease activity in cell lysates, tissue extracts, and recombinant expression systems. Its application extends to studies of gene expression, protein processing, and enzyme localization, where precise measurement of enzymatic activity is critical. Researchers leverage its sensitivity and specificity to quantify protease function under various experimental conditions, supporting investigations into cellular signaling networks and proteome dynamics.
Functional Enzyme Characterization: Z-Leu-Arg-AMC is instrumental in the functional characterization of both native and engineered proteases. Through kinetic assays and substrate specificity profiling, scientists gain a comprehensive understanding of enzyme function, catalytic mechanisms, and structural determinants of activity. The substrate's compatibility with diverse assay formats, including real-time and endpoint measurements, enables flexible experimental design and reproducible data acquisition. This facilitates comparative studies of protease variants and the evaluation of mutational effects on enzyme function.
Overall, Z-Leu-Arg-7-Amino-4-Methylcoumarin stands out as a powerful and versatile tool in protease research and enzymology. Its unique combination of substrate specificity, fluorogenic detection, and adaptability to multiple assay platforms underpins its widespread adoption in academic, pharmaceutical, and biotechnology laboratories. Whether employed for enzyme activity assays, inhibitor screening, pathway analysis, or functional characterization, this compound enables precise and efficient exploration of proteolytic processes, driving innovation in molecular and cellular research.
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