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 is a synthetic peptide substrate composed of the amino acid sequence methionine-glycine-proline conjugated to 7-amino-4-methylcoumarin (AMC), supplied as its hydrochloride salt. As a fluorogenic peptide, it is widely utilized in enzymology and biochemical research for its ability to release a highly fluorescent AMC moiety upon specific proteolytic cleavage. The design of this substrate enables sensitive detection and quantification of protease activity, particularly for enzymes that recognize and cleave at the Met-Gly-Pro motif. Its unique structure and fluorogenic properties make it a valuable tool for investigating proteolytic mechanisms, enzyme specificity, and inhibitor screening in a variety of experimental systems.
Enzyme Activity Assays: H-Met-Gly-Pro-AMC HCl is extensively employed in the development and execution of in vitro enzyme activity assays, particularly for serine and metalloproteases that target the Met-Gly-Pro sequence. Upon enzymatic cleavage, the release of AMC generates a strong fluorescent signal, facilitating real-time, quantitative measurement of protease kinetics. This approach enables researchers to determine enzyme specificity, catalytic efficiency, and substrate preferences with high sensitivity and reproducibility, supporting fundamental studies in enzymology and protein biochemistry.
High-Throughput Screening: The fluorogenic nature of this peptide substrate makes it highly suitable for high-throughput screening (HTS) applications in drug discovery and biochemical research. Its robust fluorescent readout allows for automated detection of enzymatic activity in microplate formats, streamlining the identification of potential protease inhibitors or modulators from large compound libraries. By enabling rapid and reliable data acquisition, it supports the efficient evaluation of candidate molecules and accelerates the early stages of inhibitor development.
Protease Characterization: Researchers utilize H-Met-Gly-Pro-AMC HCl to characterize the substrate specificity and cleavage preferences of target proteases. By monitoring the rate and extent of AMC release under controlled conditions, investigators can dissect the molecular determinants of protease-substrate interactions, map active site features, and compare the activity profiles of wild-type versus mutant enzymes. Such studies contribute to a deeper understanding of proteolytic regulation and the functional roles of proteases in physiological and pathological contexts.
Kinetic Analysis: The substrate's well-defined sequence and fluorogenic properties make it an ideal tool for detailed kinetic analyses of protease catalysis. By varying substrate concentrations and measuring initial reaction velocities, researchers can derive important kinetic parameters such as Km and Vmax. These data inform mechanistic models of enzyme action, support structure-activity relationship studies, and guide the rational design of synthetic substrates or inhibitors for research and industrial applications.
Inhibitor Evaluation: H-Met-Gly-Pro-AMC HCl is routinely applied in the assessment of protease inhibitor potency and selectivity. By incorporating the substrate into standardized inhibition assays, scientists can accurately quantify the effects of candidate compounds on enzymatic activity, calculate IC50 values, and distinguish between competitive and non-competitive inhibition mechanisms. This information is critical for the optimization of lead compounds and the development of selective, high-affinity protease inhibitors for further research use.
1. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
2. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs
4. Emu oil in combination with other active ingredients for treating skin imperfections
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More