Boc-Glu-Lys-Lys-AMC incorporates acidic and basic residues in a protected peptide attached to a fluorescent reporter. Its design supports investigation of protease recognition and substrate selectivity. Researchers examine its conformational and kinetic behavior. Applications include fluorescence-based assays, substrate optimization, and mechanistic evaluation.
CAT No: R2533
CAS No:73554-85-5
Synonyms/Alias:Boc-Glu-Lys-Lys-AMC;73554-85-5;BOC-GLU-LYS-LYS-MCA;Boc-Glu-Lys-Lys-Amc acetate salt;(4S)-5-[[(2S)-6-amino-1-[[(2S)-6-amino-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxohexan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-[(2-methylpropan-2-yl)oxycarbonylamino]-5-oxopentanoic acid;SCHEMBL3258147;HY-P4319;DA-61807;FB110484;CS-0653500;(S)-5-(((S)-6-amino-1-(((S)-6-amino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxohexan-2-yl)amino)-1-oxohexan-2-yl)amino)-4-((tert-butoxycarbonyl)amino)-5-oxopentanoic acid;
Boc-Glu-Lys-Lys-AMC is a synthetic peptide substrate composed of a protected glutamic acid residue, two lysine residues, and a 7-amino-4-methylcoumarin (AMC) fluorogenic tag. This compound is engineered for high specificity in enzymatic assays, particularly those targeting protease activity. Its modular peptide sequence and fluorogenic reporter make it a valuable reagent for probing proteolytic mechanisms, substrate specificity, and enzyme kinetics in a range of biochemical research settings. The inclusion of the Boc (tert-butyloxycarbonyl) group provides N-terminal protection, enhancing peptide stability and facilitating controlled experimental conditions. As a result, Boc-Glu-Lys-Lys-AMC is widely utilized in fundamental studies of protease function, inhibitor screening, and enzymology.
Protease activity assays: One of the primary applications of Boc-Glu-Lys-Lys-AMC lies in the quantitative assessment of protease activity, especially for enzymes that recognize and cleave peptide bonds adjacent to lysine or glutamic acid residues. Upon enzymatic hydrolysis, the AMC moiety is released, generating a measurable fluorescent signal. This enables sensitive, real-time monitoring of proteolytic reactions in both endpoint and kinetic formats. Researchers leverage this property to characterize enzyme specificity, determine catalytic efficiency, and compare the activity profiles of different protease isoforms under various experimental conditions.
Enzyme inhibitor screening: The fluorogenic nature of the substrate makes it ideally suited for high-throughput screening of protease inhibitors. By monitoring changes in fluorescence, scientists can rapidly evaluate the potency and selectivity of candidate compounds that modulate enzymatic activity. This approach supports the identification and optimization of novel inhibitory molecules in early-stage drug discovery and mechanistic studies, providing a robust platform for structure-activity relationship analysis and lead compound prioritization.
Substrate specificity profiling: Boc-Glu-Lys-Lys-AMC serves as a valuable tool for elucidating the substrate preferences of proteolytic enzymes. By systematically varying the peptide sequence or testing related substrates, researchers can map the recognition motifs required for efficient cleavage. This information advances understanding of enzyme-substrate interactions, informs the rational design of selective substrates, and supports the development of targeted biochemical assays for specific protease families.
Kinetic studies: The compound's well-defined peptide structure and fluorogenic response allow for precise kinetic measurements of enzymatic reactions. By quantifying the rate of AMC release under controlled conditions, investigators can calculate key parameters such as Km, Vmax, and kcat. These data are essential for comparative enzymology, mechanistic investigations, and the validation of recombinant or mutant protease preparations. The use of this substrate in kinetic analyses enhances the reproducibility and interpretability of experimental results.
Biochemical assay development: Boc-Glu-Lys-Lys-AMC is frequently employed in the development and optimization of custom biochemical assays for protease research. Its compatibility with fluorescence-based detection platforms, including microplate readers and real-time kinetic systems, enables scalable and sensitive assay formats. Researchers can tailor assay conditions to specific experimental needs, facilitating applications in basic research, enzyme engineering, and quality control workflows. The versatility of this peptide substrate underpins its widespread adoption in modern protease assay development.
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