Suc-Ala-Glu-Pro-Phe-AMC couples a succinylated tetrapeptide to a fluorogenic AMC reporter for monitoring serine-protease activity. The Pro-Phe motif provides selectivity toward chymotrypsin-like enzymes. Researchers measure fluorescence release to obtain kinetic parameters and specificity profiles. Applications include substrate screening, inhibitor evaluation, and assay development.
CAT No: R2565
CAS No:142997-30-6
Synonyms/Alias:Suc-Ala-Glu-Pro-Phe-AMC;142997-30-6;Suc-AEPF-AMC;(4S)-4-[[(2S)-2-(3-carboxypropanoylamino)propanoyl]amino]-5-[(2S)-2-[[(2S)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-5-oxopentanoic acid;MFCD01318830;HY-P4359;DA-78077;FS110578;CS-0653743;
Suc-Ala-Glu-Pro-Phe-AMC is a synthetic peptide substrate widely utilized in biochemical research, particularly in the study of protease activity. Structurally, it consists of a tetrapeptide sequence capped with a succinyl group at the N-terminus and conjugated to 7-amino-4-methylcoumarin (AMC) at the C-terminus. The presence of AMC enables sensitive fluorometric detection upon enzymatic cleavage, making this compound a valuable tool for kinetic assays and mechanistic studies of proteolytic enzymes. Its sequence specificity and fluorescent readout provide researchers with a robust platform for investigating enzyme-substrate interactions, inhibitor screening, and functional characterization of proteases.
Protease activity assays: Suc-Ala-Glu-Pro-Phe-AMC is extensively employed as a fluorogenic substrate in the quantitative analysis of protease function. Upon enzymatic cleavage at the peptide bond adjacent to the AMC moiety, free AMC is released, resulting in a measurable increase in fluorescence. This property allows for the real-time monitoring of protease kinetics in solution, facilitating the determination of enzyme specificity, catalytic efficiency, and substrate preference. The substrate's sequence has been optimized for sensitivity to particular protease classes, making it suitable for detailed enzymological investigations.
Enzyme inhibitor screening: The substrate's fluorogenic nature makes it highly effective for high-throughput screening of protease inhibitors. By providing a rapid, quantifiable readout of enzymatic activity, Suc-Ala-Glu-Pro-Phe-AMC enables researchers to assess the potency and selectivity of candidate inhibitory compounds. This application is critical in the early stages of drug discovery and in the development of chemical probes for dissecting protease function in complex biological systems. The sensitivity of the fluorescence assay supports precise determination of inhibition constants and mode-of-action studies.
Substrate specificity profiling: Researchers utilize this peptide to probe the substrate recognition characteristics of various proteases. By analyzing the rate and extent of AMC release in the presence of different enzymes, it is possible to delineate the sequence preferences and cleavage site selectivity of target proteases. This information is essential for elucidating enzyme function, mapping active site architecture, and guiding the rational design of selective substrates or inhibitors for further biochemical applications.
Biochemical pathway elucidation: The substrate's design allows it to serve as a molecular probe in studies aimed at mapping proteolytic pathways within cellular or tissue extracts. By monitoring the generation of fluorescent AMC, investigators can identify the presence and activity of specific proteolytic enzymes under various experimental conditions. This approach aids in the dissection of complex protease networks, supports the identification of regulatory mechanisms, and contributes to a deeper understanding of protein turnover and processing in biological systems.
Assay development and optimization: Suc-Ala-Glu-Pro-Phe-AMC is frequently incorporated into the development of robust, reproducible assay systems for both academic and industrial research settings. Its consistent performance, sensitivity, and compatibility with automated fluorescence detection platforms make it an ideal choice for optimizing assay parameters, validating new protocols, and standardizing enzyme activity measurements across different laboratories. The use of this substrate streamlines the process of assay calibration and ensures reliable data generation for downstream applications.
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