Boc-Leu-Lys-Arg-AMC Hydrochloride Salt combines a protected tripeptide with an AMC fluorophore for trypsin-like protease assays. Leucine provides hydrophobic contacts, while lysine and arginine define strong basic recognition features. The hydrochloride salt enhances aqueous solubility and handling. Researchers monitor fluorescence release to characterize catalytic efficiency, specificity, and inhibitor potency.
CAT No: R2605
CAS No:109358-47-6
Synonyms/Alias:109358-47-6;Boc-Leu-Lys-Arg-AMC;BOC-LEU-LYS-ARG-AMC HYDROCHLORIDE SALT;Boc-Leu-Lys-Arg-Mca;tert-butyl N-[(2S)-1-[[(2S)-6-amino-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate;CHEMBL3142582;DTXSID401111490;HY-P4312;DA-51302;FB110554;CS-0653485;N-[(1,1-Dimethylethoxy)carbonyl]-L-leucyl-L-lysyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-L-argininamide;tert-butyl ((S)-1-(((S)-6-amino-1-(((S)-5-guanidino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxopentan-2-yl)amino)-1-oxohexan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)carbamate;tert-butyl (S)-1-((S)-6-amino-1-((S)-5-guanidino-1-(4-methyl-2-oxo-2H-chromen-7-ylamino)-1-oxopentan-2-ylamino)-1-oxohexan-2-ylamino)-4-methyl-1-oxopentan-2-ylcarbamate;TERT-BUTYL N-[(1S)-1-{[(1S)-5-AMINO-1-{[(1S)-4-CARBAMIMIDAMIDO-1-[(4-METHYL-2-OXOCHROMEN-7-YL)CARBAMOYL]BUTYL]CARBAMOYL}PENTYL]CARBAMOYL}-3-METHYLBUTYL]CARBAMATE;
Boc-Leu-Lys-Arg-AMC hydrochloride salt is a synthetic peptide substrate widely recognized for its versatility in biochemical research and assay development. Featuring a unique sequence of leucine, lysine, and arginine residues capped with a 7-amino-4-methylcoumarin (AMC) fluorophore, this compound is designed for sensitive detection and quantification of proteolytic enzyme activity. The presence of the Boc (tert-butyloxycarbonyl) protecting group enhances its stability during storage and handling, while the hydrochloride salt form ensures excellent solubility in aqueous solutions. Its structure allows for precise cleavage by specific proteases, releasing the highly fluorescent AMC moiety, which can be easily monitored in real-time using fluorescence-based detection methods. Researchers value this substrate for its high sensitivity, rapid response, and compatibility with a wide range of experimental conditions, making it a reliable tool in enzymology and molecular biology laboratories.
Protease Activity Assays: Boc-Leu-Lys-Arg-AMC hydrochloride salt serves as a preferred substrate for quantifying serine and cysteine protease activity in vitro. Upon enzymatic cleavage, the AMC group is liberated, resulting in a measurable fluorescence increase that directly correlates with proteolytic activity. This enables precise kinetic studies, inhibitor screening, and enzyme characterization in various biological samples, including cell lysates, tissue extracts, and purified protein preparations. The substrate's specificity for certain protease recognition sequences allows researchers to distinguish between closely related enzyme families, facilitating the development of selective inhibitors and the elucidation of protease function in complex biological systems.
Drug Discovery and High-Throughput Screening: In pharmaceutical research, Boc-Leu-Lys-Arg-AMC is a valuable asset for high-throughput screening (HTS) platforms aimed at identifying novel protease inhibitors or modulators. Its robust fluorescence signal and compatibility with automated liquid handling systems make it ideal for large-scale compound library screening. By enabling rapid and sensitive detection of enzyme activity changes, the substrate accelerates lead identification and optimization processes in early-stage drug discovery. Furthermore, its use in secondary assays helps validate hit compounds and assess their selectivity profiles against target proteases.
Enzyme Mechanism Studies: The peptide substrate is instrumental in dissecting the catalytic mechanisms of proteolytic enzymes. By providing a defined cleavage site and a quantifiable fluorescent readout, it allows for detailed analysis of enzyme kinetics, substrate specificity, and active site interactions. Researchers can employ it to investigate the effects of site-directed mutagenesis, post-translational modifications, or environmental factors on protease function. Such mechanistic insights are critical for understanding enzyme regulation and for designing targeted interventions in pathological processes involving dysregulated proteolysis.
Biomarker Research and Diagnostics: Boc-Leu-Lys-Arg-AMC hydrochloride salt contributes to the identification and validation of protease-based biomarkers in biological fluids and tissue samples. Its high sensitivity enables the detection of subtle changes in protease activity associated with physiological or pathological states, supporting the development of diagnostic assays and monitoring tools. The substrate can be incorporated into multiplexed assay formats, allowing simultaneous measurement of multiple enzyme activities and providing comprehensive profiles of proteolytic landscapes in health and disease.
Cellular and Molecular Biology Studies: In cell biology, the substrate is frequently used to monitor intracellular or extracellular protease activity in live or fixed cells. By tracking AMC fluorescence, scientists can visualize spatial and temporal patterns of proteolysis, investigate signaling pathways, and assess the effects of genetic or pharmacological perturbations. Its application extends to studies of apoptosis, cell migration, and tissue remodeling, where protease activity plays pivotal regulatory roles. The non-toxic nature of the released AMC fluorophore ensures minimal interference with cellular processes, enabling accurate and reproducible measurements in diverse experimental models.
Peptide-based substrate research: Boc-Leu-Lys-Arg-AMC hydrochloride salt is also a reference compound in the ongoing development of novel peptide-based substrates for protease assays. Its well-characterized properties and predictable cleavage profile provide a benchmark for evaluating the performance of new substrate designs. Researchers utilize it to compare fluorescence intensity, signal-to-noise ratio, and kinetic parameters, guiding the optimization of assay sensitivity and specificity. The substrate's widespread adoption in both academic and industrial settings underscores its enduring value as a foundational tool in protease research and assay innovation.
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