Ac-Leu-Arg-AMC is a fluorogenic peptide substrate.
CAT No: R1149
CAS No:929621-79-4
Synonyms/Alias:Ac-Leu-Arg-AMC;929621-79-4;(2S)-2-acetamido-N-[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]-4-methylpentanamide;DTXSID501150013;HY-P1448;DA-60770;MS-29041;PD099883;CS-0034435;G16226;N-Acetyl-L-leucyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-L-argininamide;(S)-2-Acetamido-N-((S)-5-guanidino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxopentan-2-yl)-4-methylpentanamide;
Ac-Leu-Arg-AMC, also known as N-Acetyl-Leucyl-Arginyl-7-amino-4-methylcoumarin, is a synthetic peptide substrate widely employed in enzymology and protease research. Structurally, it comprises an N-acetylated dipeptide sequence (leucine-arginine) conjugated to the fluorogenic moiety 7-amino-4-methylcoumarin (AMC). This configuration enables sensitive detection of proteolytic activity, as enzymatic cleavage releases the highly fluorescent AMC group. The compound's design makes it particularly valuable for investigating the specificity and kinetics of serine and cysteine proteases, as well as for developing robust biochemical assays. Its utility extends across a broad range of applications in fundamental research, drug discovery, and high-throughput screening environments.
Protease activity assays: As a fluorogenic peptide substrate, Ac-Leu-Arg-AMC is extensively utilized in the quantitative measurement of protease activity, especially for enzymes such as trypsin-like serine proteases and certain cysteine proteases. Upon enzymatic hydrolysis at the arginine-AMC bond, the liberated AMC fluorophore emits a strong fluorescent signal, allowing for real-time monitoring of proteolytic reactions. This property enables highly sensitive detection and kinetic analysis of enzyme activity in both purified enzyme systems and complex biological samples.
Enzyme specificity profiling: The dipeptide sequence within this substrate is tailored to probe the substrate preferences of various proteases. Researchers employ it to characterize the cleavage specificity and substrate recognition profiles of target enzymes, facilitating the identification of optimal peptide sequences for further assay development. By comparing the hydrolysis rates of this and related substrates, insights into enzyme selectivity and catalytic mechanisms can be obtained, which are critical for understanding protease function in physiological and pathological contexts.
High-throughput screening: The robust fluorescence response of AMC release makes this substrate highly suitable for automated high-throughput screening (HTS) of protease inhibitors or activators. In drug discovery pipelines, it serves as a reliable reporter in microplate-based assays, enabling rapid and reproducible assessment of compound libraries for modulatory effects on protease activity. Its compatibility with standard fluorescence plate readers streamlines assay setup and data acquisition, supporting efficient identification of lead molecules.
Kinetic studies and mechanistic analysis: The well-defined chemical structure and consistent fluorescence output of Ac-Leu-Arg-AMC allow for precise kinetic measurements of enzyme-catalyzed reactions. Researchers leverage this substrate to determine key enzymatic parameters, such as Km and Vmax, and to investigate catalytic efficiency and inhibition mechanisms. These quantitative insights are essential for elucidating enzyme function, guiding rational inhibitor design, and validating assay conditions for downstream applications.
Biochemical assay development: The versatility and sensitivity of this fluorogenic peptide make it a preferred choice in the development of novel biochemical assays tailored to specific proteases. Its use spans basic research, where it aids in dissecting proteolytic pathways, as well as applied settings, such as quality control in bioprocessing or screening of enzyme variants. The substrate's modular design also permits adaptation to multiplexed formats or integration into more complex assay platforms, enhancing the analytical capabilities available to researchers and industry professionals alike.
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