Z-Gly-Pro-Arg-AMC HCl combines a protected peptide motif with an AMC fluorophore to support detection of proteolytic activity. Glycine and proline shape turn formation, while arginine provides strong electrostatic interactions. Researchers evaluate its cleavage kinetics and fluorescence behavior. Applications include enzyme assays, substrate optimization, and mechanistic studies.
CAT No: R2476
CAS No:201928-42-9
Synonyms/Alias:201928-42-9;Z-Gly-Pro-Arg-AMC HCl;Z-Gly-Pro-Arg-AMC.HCl;Z-Gly-Pro-Arg-AMC (hydrochloride);Z-Gly-Pro-Arg-Mca Hydrochloride;benzyl N-[2-[(2S)-2-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-2-oxoethyl]carbamate;hydrochloride;Z-Gly-pro-arg-amc hydrochloride;WIIZWHSOXXZHRC-UKOKCHKQSA-N;HY-P4217;MFCD00077020;FG110494;CS-0650897;Benzyl (2-((S)-2-(((S)-5-guanidino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxopentan-2-yl)carbamoyl)pyrrolidin-1-yl)-2-oxoethyl)carbamate hydrochloride;benzyl 2-((S)-2-((S)-5-guanidino-1-(4-methyl-2-oxo-2H-chromen-7-ylamino)-1-oxopentan-2-ylcarbamoyl)pyrrolidin-1-yl)-2-oxoethylcarbamate hydrochloride;BENZYL N-{2-[(2S)-2-{[(1S)-4-CARBAMIMIDAMIDO-1-[(4-METHYL-2-OXOCHROMEN-7-YL)CARBAMOYL]BUTYL]CARBAMOYL}PYRROLIDIN-1-YL]-2-OXOETHYL}CARBAMATE HYDROCHLORIDE;L-Argininamide,N-[(phenylmethoxy)carbonyl]glycyl-L-prolyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-,monohydrochloride(9ci);
Z-Gly-Pro-Arg-AMC HCl is a synthetic peptide substrate widely recognized for its utility in enzymology and biochemical research. Structurally, it features a tripeptide sequence (Glycine-Proline-Arginine) capped at the N-terminus with a benzyloxycarbonyl (Z) group and at the C-terminus with the fluorogenic 7-amino-4-methylcoumarin (AMC) moiety, presented as the hydrochloride salt. This design enables sensitive detection of proteolytic cleavage events, particularly those mediated by serine proteases such as thrombin or trypsin-like enzymes. The release of the AMC fluorophore upon enzymatic cleavage provides a robust and quantifiable signal, making the compound indispensable for kinetic studies, inhibitor screening, and mechanistic investigations in protease research.
Enzyme activity assays: Z-Gly-Pro-Arg-AMC HCl serves as a highly effective substrate for the quantitative measurement of protease activity, especially for enzymes exhibiting trypsin-like or thrombin-like specificity. Upon enzymatic hydrolysis of the peptide bond adjacent to the AMC group, free AMC is liberated, resulting in a measurable fluorescence increase. This property allows researchers to monitor proteolytic activity in real time, facilitating the study of enzyme kinetics, substrate specificity, and catalytic efficiency under various experimental conditions.
Inhibitor screening: The fluorogenic response of this peptide substrate is particularly advantageous in high-throughput screening assays designed to identify and characterize protease inhibitors. By measuring changes in fluorescence, researchers can rapidly assess the inhibitory potency of candidate compounds against targeted serine proteases. This approach streamlines the discovery and optimization of novel inhibitors for use in biochemical research or drug development pipelines, providing a sensitive and reproducible readout for compound efficacy.
Mechanistic enzymology: Z-Gly-Pro-Arg-AMC HCl is frequently employed in mechanistic studies to dissect the catalytic mechanisms of serine proteases. By enabling precise measurement of reaction rates and substrate turnover, it supports detailed analyses of enzyme-substrate interactions, transition state stabilization, and the influence of cofactors or allosteric modulators. Such insights are essential for elucidating fundamental principles of enzyme catalysis and for informing rational design of enzyme variants with altered specificity or activity.
Biochemical pathway analysis: The substrate's specificity for certain proteolytic enzymes makes it a valuable probe in mapping protease activities within complex biological samples, such as cell lysates or tissue extracts. By selectively monitoring the activity of target enzymes, researchers can investigate proteolytic processing events, regulatory mechanisms, and pathway dynamics in physiological or experimental contexts. This capability contributes to a deeper understanding of protease function in cellular signaling, protein turnover, and disease-related processes.
Analytical method development: The robust and sensitive fluorescence-based detection enabled by Z-Gly-Pro-Arg-AMC HCl underpins its use in the development and validation of analytical methods for protease quantification. Its compatibility with microplate readers and automated liquid handling systems supports the creation of scalable, reproducible assays suitable for laboratory automation and high-throughput workflows. Such methods are integral to quality control, enzyme characterization, and the standardization of protease assays across diverse research and industrial settings.
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