H-Gly-Arg-AMC links a minimal dipeptide recognition element to an AMC fluorophore, forming a sensitive substrate for trypsin-like proteases. The arginine residue defines cleavage specificity, while glycine provides flexibility. Researchers quantify fluorescence increase to monitor catalytic turnover. Applications include high-throughput screening, kinetic analysis, and protease-mechanism research.
CAT No: R2570
CAS No:65147-19-5
Synonyms/Alias:H-Gly-Arg-AMC;Gly-Arg-AMC;65147-19-5;(2S)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)-N-(4-methyl-2-oxochromen-7-yl)pentanamide;Gly-Arg-7-Amino-4-Methylcoumarin;glycyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-L-argininamide, hydrochloride;70274-78-1;(S)-2-(2-Aminoacetamido)-5-guanidino-N-(4-methyl-2-oxo-2H-chromen-7-yl)pentanamide;H-Gly-Arg-AMC hydrochloride salt;Gly-Arg-AMC (hydrochloride);CHEMBL65584;SCHEMBL7574189;HY-P4342;FG110503;CS-0653705;(2S)-2-[(2-aminoacetyl)amino]-5-guanidino-N-(4-methyl-2-oxo-chromen-7-yl)pentanamide;
H-Gly-Arg-AMC is a synthetic peptide substrate widely utilized in biochemical research for its role in fluorogenic enzymatic assays. Structurally, it consists of a dipeptide, glycine-arginine, conjugated to 7-amino-4-methylcoumarin (AMC), a well-established fluorophore. Upon enzymatic cleavage, AMC is released, generating a fluorescent signal that enables sensitive detection and quantification of protease activity. This compound's modular design and robust fluorescence properties make it an essential reagent for exploring proteolytic mechanisms, characterizing enzyme specificity, and supporting high-throughput screening workflows in academic and industrial laboratories.
Protease activity assays: H-Gly-Arg-AMC is extensively employed as a fluorogenic substrate for the measurement of serine and cysteine protease activities, particularly those with trypsin-like specificity. When acted upon by target enzymes, the peptide bond between arginine and AMC is cleaved, liberating free AMC and resulting in a quantifiable increase in fluorescence. This sensitive readout allows researchers to monitor enzyme kinetics in real time, facilitating detailed studies of catalytic efficiency, substrate specificity, and inhibitor potency in a variety of experimental systems.
Enzyme inhibitor screening: The compound is a valuable tool for high-throughput screening of protease inhibitors. By providing a rapid and reliable fluorescence-based assay format, it enables the identification and characterization of small molecules or biologics that modulate protease function. Such screening is critical in early-stage drug discovery and for elucidating the molecular basis of protease regulation, as it permits efficient comparison of candidate inhibitors under standardized conditions.
Substrate specificity profiling: H-Gly-Arg-AMC serves as a model substrate for profiling the substrate preferences of proteases. By comparing the rate of AMC release among different enzyme preparations or under varied assay conditions, researchers can dissect the structural determinants of substrate recognition. This information is crucial for understanding enzyme function at the molecular level and for engineering proteases with tailored specificity for biotechnological applications.
Kinetic characterization of enzymatic reactions: The fluorogenic properties of the AMC moiety allow for precise kinetic measurements of proteolytic reactions. Using this substrate, investigators can determine key enzymatic parameters such as Km and Vmax, assess the effects of mutations or cofactors, and compare the catalytic properties of wild-type and engineered enzymes. The continuous, real-time fluorescence readout streamlines data acquisition and enhances the reproducibility of kinetic analyses.
Quality control and process monitoring: In industrial and bioprocessing contexts, H-Gly-Arg-AMC is utilized to monitor protease activity in complex mixtures, such as fermentation broths or cell lysates. Its sensitivity and specificity enable detection of trace proteolytic contaminants or assessment of protease levels during purification and production workflows. This application supports quality assurance efforts by providing rapid, quantitative insights into enzymatic activity, thereby ensuring consistency and reliability in biomanufacturing processes.
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