H-Met-Gly-Pro-AMC HCl features a tripeptide linked to a fluorogenic coumarin derivative for monitoring enzymatic cleavage. Methionine contributes redox sensitivity, while proline induces conformational constraints. Researchers utilize fluorescence release to study catalytic pathways. Uses include protease assays, kinetic mapping, and substrate profiling.
CAT No: R2712
CAS No:1926163-53-2
Synonyms/Alias:H-Met-Gly-Pro-AMC HCl;1926163-53-2;(2S)-1-[2-[[(2S)-2-amino-4-methylsulfanylbutanoyl]amino]acetyl]-N-(4-methyl-2-oxochromen-7-yl)pyrrolidine-2-carboxamide;hydrochloride;H-Met-Gly-Pro-AMC inverted exclamation mark currencyHCl;H-Met-Gly-Pro-AMC.HCl;MFCD03424233;FM110594;
H-Met-Gly-Pro-AMC HCl, also known as Methionyl-Glycyl-Prolyl-7-amino-4-methylcoumarin hydrochloride, is a synthetic peptide substrate widely utilized in biochemical research and enzymology. This compound features a peptide backbone conjugated to a fluorescent AMC (7-amino-4-methylcoumarin) moiety, making it especially valuable for fluorescence-based enzymatic assays. Its unique structure enables researchers to monitor protease activity in real time, as the cleavage of the peptide bond releases the AMC group, resulting in a measurable fluorescent signal. The hydrochloride salt form enhances its solubility and stability in aqueous environments, facilitating its integration into diverse experimental protocols. H-Met-Gly-Pro-AMC HCl is recognized for its specificity and sensitivity in detecting enzymatic activity, supporting a wide range of studies in protease function, inhibitor screening, and kinetic analysis.
Enzyme Activity Assays: H-Met-Gly-Pro-AMC HCl is extensively employed in quantifying protease activity, particularly for enzymes that recognize the Met-Gly-Pro sequence. By incorporating this substrate into enzymatic reactions, researchers can assess the catalytic efficiency and substrate specificity of target proteases. The release of the fluorescent AMC group upon enzymatic cleavage provides a sensitive and non-radioactive method for continuous monitoring, enabling precise kinetic measurements and facilitating the characterization of enzyme mechanisms under various conditions.
Protease Inhibitor Screening: The fluorescent properties of this peptide substrate make it an ideal tool for high-throughput screening of protease inhibitors. In pharmaceutical and academic research, H-Met-Gly-Pro-AMC HCl is used to evaluate the efficacy of small molecules or biological inhibitors by measuring their capacity to prevent substrate cleavage. This approach streamlines the identification and optimization of novel compounds with therapeutic potential, supporting drug discovery efforts that target proteolytic enzymes implicated in diverse physiological and pathological processes.
Biochemical Pathway Elucidation: Methionyl-Glycyl-Prolyl-AMC substrates contribute to the investigation of biochemical pathways involving proteolytic processing. By introducing this substrate into cell-free systems or tissue extracts, scientists can track the activity of endogenous proteases and map their roles within complex metabolic networks. The real-time fluorescence readout enables dynamic studies of protease regulation, substrate turnover, and pathway modulation, advancing our understanding of cellular homeostasis and protein life cycles.
Enzyme Kinetics and Mechanistic Studies: Researchers utilize H-Met-Gly-Pro-AMC HCl to perform detailed kinetic analyses of proteolytic reactions. The substrate's design allows for the determination of key parameters such as Km and Vmax, offering insights into enzyme-substrate interactions and catalytic mechanisms. By varying substrate concentrations and experimental conditions, scientists can dissect the influence of cofactors, inhibitors, or mutations on enzymatic function, contributing to fundamental knowledge in enzymology and protein chemistry.
Fluorescence-Based Detection Systems: The AMC fluorophore released from this substrate upon enzymatic cleavage serves as a robust reporter in fluorescence-based detection systems. Laboratories employ it in microplate assays, flow cytometry, and other analytical platforms to achieve high sensitivity and specificity in protease detection. Its compatibility with automated instrumentation and multiplexed assays supports large-scale studies and comparative analyses, making it a valuable asset in both basic research and applied bioscience.
Research utilizing H-Met-Gly-Pro-AMC HCl continues to expand, with ongoing innovations in assay development and enzyme characterization. Its versatility as a fluorescent substrate underpins advances in protease research, inhibitor discovery, and the elucidation of complex biochemical pathways. As scientists seek to unravel the intricacies of proteolytic regulation and function, this compound remains a cornerstone in the toolkit for enzymology and molecular biology, fostering progress across multiple disciplines and experimental approaches.
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