MCA-SEVNLDAEFR-K(Dnp)-RR, amide is a FRET-based substrate.
CAT No: R1509
CAS No:438625-61-7
Synonyms/Alias:438625-61-7;FM110959;Mca-(Asn670,Leu671)-Amyloid beta/A4 Protein Precursor770 (667-676)-Lys(Dnp)-Arg-Arg amide trifluoroacetate salt;Mca-(Asn670,Leu671)-Amyloid beta/A4 Protein Precursor770(667-676)-Lys(Dnp)-Arg-Arg amide;
MCA-SEVNLDAEFR-K(Dnp)-RR, amide is a synthetic peptide substrate engineered for high specificity in protease research, particularly in the study of β-secretase (BACE1) activity. Featuring a sequence derived from the amyloid precursor protein (APP) and labeled with both a fluorescent donor (MCA) and a quencher (Dnp), this peptide enables efficient detection of proteolytic cleavage events via fluorescence resonance energy transfer (FRET). Its design allows researchers to monitor enzyme kinetics in real time, making it a valuable tool in neurodegenerative disease research and drug discovery targeting proteolytic pathways.
Protease activity assays: As a FRET-based peptide substrate, MCA-SEVNLDAEFR-K(Dnp)-RR, amide is widely employed in the quantitative analysis of protease activity, especially for β-secretase (BACE1). Upon enzymatic cleavage at the specific recognition site, the proximity between the MCA fluorophore and Dnp quencher is disrupted, resulting in a measurable increase in fluorescence. This feature facilitates sensitive and continuous monitoring of protease kinetics in vitro, supporting the characterization of enzyme specificity, substrate affinity, and catalytic efficiency under various experimental conditions.
Inhibitor screening: The peptide serves as a robust platform for high-throughput screening of small-molecule or peptide-based inhibitors targeting BACE1 and related aspartyl proteases. By providing a direct and quantifiable readout of enzyme inhibition through changes in fluorescence intensity, it streamlines the identification and evaluation of potential lead compounds. This application is essential for early-stage drug discovery programs focused on modulating proteolytic processing implicated in neurodegenerative disorders.
Enzyme mechanism studies: Utilizing the precise sequence and dual-label design, researchers can dissect the mechanistic aspects of substrate recognition and cleavage by BACE1 and other proteases. The substrate enables detailed investigation into enzyme-substrate interactions, cleavage site specificity, and the influence of sequence modifications on catalytic activity. Such studies contribute to a deeper understanding of protease function and regulation within complex biological systems.
Kinetic parameter determination: The peptide's well-characterized cleavage site and fluorescent properties make it ideal for determining key kinetic parameters, such as Km and Vmax, for BACE1 and related enzymes. Researchers can perform Michaelis-Menten analyses and other kinetic studies to elucidate enzyme efficiency and to compare the effects of mutations, cofactors, or environmental variables on proteolytic activity. These insights are crucial for both fundamental enzymology and applied research in inhibitor optimization.
Assay development and optimization: The versatility and sensitivity of MCA-SEVNLDAEFR-K(Dnp)-RR, amide support its use in the development and refinement of biochemical assays for protease detection. Its compatibility with various detection platforms, including microplate readers and automated screening systems, allows for scalable assay design tailored to specific research needs. The substrate's performance characteristics facilitate the establishment of robust, reproducible protocols for both basic research and industrial applications in enzymology and drug screening.
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