An excellent fluorogenic substrate for measuring the peptidylglutamyl-peptide-hydrolyzing (PGPH) activity of the 20S proteasome, which is excited at 340-360 nm and emits at 440-460 nm. It is typically used in cell lysates after experimental treatment.
CAT No: R1025
CAS No:348086-66-8
Synonyms/Alias:Z-Leu-Leu-Glu-AMC;348086-66-8;Z-LLE-AMC;Cbz-Leu-Leu-Glu-AMC;(5S,8S,11S)-5,8-Diisobutyl-11-((4-methyl-2-oxo-2H-chromen-7-yl)carbamoyl)-3,6,9-trioxo-1-phenyl-2-oxa-4,7,10-triazatetradecan-14-oic acid;(4S)-4-[[(2S)-4-methyl-2-[[(2S)-4-methyl-2-(phenylmethoxycarbonylamino)pentanoyl]amino]pentanoyl]amino]-5-[(4-methyl-2-oxochromen-7-yl)amino]-5-oxopentanoic acid;Z-Leu-Leu-Glu-MCA;Z-Leu-Leu-Glu-7-Amino-4-Methylcoumarin;Z-Leu-Leu-Glu-AMC [Z-LLE-AMC];MFCD01074989;Z-LEU-LEU-GLU-7-AMIDO-4-METHYLCOUMARIN;Z-L-Leu-L-Leu-L-Glu-AMC;SCHEMBL15569405;CHEBI:229563;AKOS027327743;Proteasome Substrate II (Fluorogenic);NCGC00485335-01;FL110601;HY-123053;CS-0081090;Z-Leu-Leu-Glu-7-amido-4-methylcoumarin, >=95%, solid;(4S)-4-[(2S)-2-[(2S)-2-{[(BENZYLOXY)CARBONYL]AMINO}-4-METHYLPENTANAMIDO]-4-METHYLPENTANAMIDO]-4-[(4-METHYL-2-OXOCHROMEN-7-YL)CARBAMOYL]BUTANOIC ACID;(5S,8S,11S)-5,8-Diisobutyl-11-((4-methyl-2-oxo-2H-chromen-7-yl)carbamoyl)-3,6,9-trioxo-1-phenyl-2-oxa-4,7,10-triazatetradecan-14-oicacid;N-[(benzyloxy)carbonyl]-L-leucyl-L-leucyl-N-(4-methyl-2-oxo-2H-chromen-7-yl)-L-alpha-glutamine;
Z-Leu-Leu-Glu-AMC is a synthetic peptide substrate widely utilized in biochemical research for the assessment of protease activity, particularly for enzymes that recognize and cleave specific peptide sequences. Structurally, it consists of a tripeptide chain—leucine-leucine-glutamic acid—protected at the N-terminus with a benzyloxycarbonyl (Z) group and conjugated at the C-terminus to 7-amino-4-methylcoumarin (AMC), a fluorogenic reporter. This design enables sensitive, real-time detection of enzymatic cleavage events via fluorescence, making it a valuable tool in enzymology, drug discovery, and mechanistic studies of proteolytic pathways.
Enzyme activity assays: Z-Leu-Leu-Glu-AMC is predominantly applied in the quantitative measurement of protease activity, most notably for enzymes such as caspases, cathepsins, and other serine or cysteine proteases that recognize the Leu-Leu-Glu motif. Upon enzymatic cleavage, the AMC moiety is released, resulting in a marked increase in fluorescence that can be monitored spectroscopically. This property enables precise kinetic analysis of enzyme activity in cell lysates, purified protein systems, or high-throughput screening platforms, facilitating the identification and characterization of protease function under various experimental conditions.
Drug discovery and inhibitor screening: The fluorogenic nature of this peptide substrate makes it highly suitable for use in drug discovery pipelines, where it serves as a reliable readout for high-throughput screening of protease inhibitors. By enabling rapid and sensitive detection of enzyme inhibition, it supports the identification of novel small-molecule modulators or peptide-based inhibitors with potential applications in the study of protease-related pathways. The use of Z-Leu-Leu-Glu-AMC in these assays allows for efficient ranking of compound potency and selectivity, streamlining early-stage lead optimization.
Biochemical mechanism elucidation: Researchers employ this substrate to investigate the substrate specificity and catalytic mechanisms of various proteases. By analyzing cleavage rates and patterns in the presence of different enzyme variants, cofactors, or environmental conditions, it is possible to gain insights into the structural determinants of enzyme-substrate recognition. Such studies contribute to a deeper understanding of protease regulation, activation, and inhibition, which is critical for elucidating their roles in physiological and pathological processes.
Protease profiling in complex samples: The substrate's compatibility with fluorescence-based detection systems allows for its use in profiling protease activity within complex biological samples, such as tissue extracts or cell lysates. This application is valuable for comparative analyses of proteolytic activity across different biological states, including developmental stages, disease models, or treatment conditions. The ability to monitor protease activity in situ provides researchers with a powerful approach to studying dynamic biochemical processes in a physiologically relevant context.
Method development and assay optimization: Z-Leu-Leu-Glu-AMC is frequently used in the development and optimization of novel assay formats for protease research. Its well-characterized cleavage properties and robust fluorescent response enable assay designers to refine buffer conditions, substrate concentrations, and detection parameters for maximal sensitivity and reproducibility. In addition, it serves as a benchmark standard for validating new analytical platforms or instrumentation, ensuring consistent and reliable performance in protease-related studies.
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