Boc-Leu-Gly-Arg-AMC is a fluorogenic AMC substrate for the convertases. Boc-Leu-Gly-Arg-AMC can be used in enzymatic assays.
CAT No: 10-101-299
CAS No:65147-09-3
Synonyms/Alias:Boc-Leu-Gly-Arg-AMC;65147-09-3;Boc-Leu-Gly-Arg-Mca;tert-butyl N-[(2S)-1-[[2-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-4-methyl-1-oxopentan-2-yl]carbamate;BOC-LEU-GLY-ARG-AMC ACETATE SALT;HY-P2237;AKOS040764220;DA-71642;FB110486;MS-30623;Boc-Leu-Gly-Arg-4-methyl-coumaryl-7-amide;CS-0114663;G12102;tert-butyl ((S)-1-((2-(((S)-5-guanidino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxopentan-2-yl)amino)-2-oxoethyl)amino)-4-methyl-1-oxopentan-2-yl)carbamate;tert-butyl (S)-1-(2-((S)-5-guanidino-1-(4-methyl-2-oxo-2H-chromen-7-ylamino)-1-oxopentan-2-ylamino)-2-oxoethylamino)-4-methyl-1-oxopentan-2-ylcarbamate;
Chemical Name:tert-butyl N-[(2S)-1-[[2-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-4-methyl-1-oxopentan-2-yl]carbamate
Boc-Leu-Gly-Arg-AMC is a synthetic peptide substrate widely utilized in biochemical research for its fluorogenic properties and its utility in enzymatic activity assays. Structurally, it features a protected N-terminus with a tert-butyloxycarbonyl (Boc) group and a C-terminal 7-amino-4-methylcoumarin (AMC) moiety, which enables sensitive detection upon enzymatic cleavage. The peptide sequence itself, Leu-Gly-Arg, is specifically designed to be recognized and hydrolyzed by certain proteases, making this compound a valuable tool for investigating proteolytic mechanisms, enzyme specificity, and related biochemical processes. Its unique combination of sequence specificity and fluorogenic reporting positions it as a critical reagent in studies of protease function, inhibitor screening, and kinetic characterization.
Protease activity assays: In enzymology laboratories, Boc-Leu-Gly-Arg-AMC is extensively employed as a fluorogenic substrate to monitor the activity of serine proteases, particularly those with trypsin-like specificity. Upon enzymatic cleavage at the arginine residue, the AMC group is released, resulting in a quantifiable fluorescence signal. This enables researchers to conduct real-time kinetic studies, determine enzyme activity levels, and compare the catalytic efficiency of various protease isoforms or mutants under different conditions. The high sensitivity of AMC fluorescence detection supports applications requiring precise measurement of low-abundance enzymes or subtle changes in proteolytic activity.
Enzyme inhibitor screening: The substrate is frequently used in high-throughput screening platforms to identify and characterize inhibitors of serine proteases. By measuring the reduction in AMC fluorescence upon addition of potential inhibitory compounds, researchers can rapidly evaluate the potency and specificity of novel inhibitors. This application is particularly relevant in drug discovery and basic research focused on regulatory pathways involving proteolytic enzymes, as it provides a robust and quantitative method for assessing inhibitor efficacy and selectivity.
Substrate specificity profiling: Boc-Leu-Gly-Arg-AMC serves as a model substrate for mapping the substrate preferences of proteases. By comparing the rate and extent of hydrolysis with those of other peptide-AMC conjugates, investigators can elucidate the structural determinants of enzyme-substrate recognition. This approach is critical for understanding the molecular basis of protease selectivity, guiding the rational design of selective substrates or inhibitors, and informing the development of diagnostic assays that exploit unique protease signatures.
Biochemical pathway elucidation: The compound is a valuable probe in studies aiming to delineate protease-mediated signaling pathways or degradation processes. By tracking the cleavage of this substrate in complex biological samples, such as cell lysates or tissue extracts, researchers can identify active proteases, monitor changes in proteolytic profiles under different experimental conditions, and investigate the regulation of protease activity in response to physiological or pathological stimuli. This contributes to a deeper understanding of cellular proteostasis and the dynamic roles of proteolytic enzymes in health and disease.
Analytical method development: In analytical biochemistry, Boc-Leu-Gly-Arg-AMC is used to validate and optimize fluorometric assay protocols for protease detection. Its well-characterized cleavage and fluorescence properties make it a standard reference substrate for calibrating assay sensitivity, establishing detection limits, and benchmarking the performance of instrumentation. This supports the development of reliable, reproducible, and high-throughput analytical workflows for enzyme quantification in a variety of research and industrial settings.
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