Decanoyl-RVKR-CMK is highly specific, potent, irreversible, and cell-permeable competitive subtilisin/kex2p-like proprotein convertase inhibitor. It can inhibit activity of all seven convertases (pc1, pc2, pc4, pace4, pc5, pc7 and furin). It is used as a useful antiviral agent.
CAT No: R0888
CAS No:150113-99-8
Synonyms/Alias:Decanoyl-RVKR-CMK;150113-99-8;DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE;Dec-RVKR-CMK;Furin-IN-I;N-[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(3S)-1-chloro-6-(diaminomethylideneamino)-2-oxohexan-3-yl]amino]-1-oxohexan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]decanamide;decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone;decanoyl-Arg-Val-Lys-Arg-CMK;Furin Inhibitor I;Decanoyl-Arg-Val-Lys-Arg-chloromethylketone trifluoroacetate salt;decanoyl-RVKR-chloromethylketone;GTPL11258;CHEBI:156289;AKOS024457645;DA-62736;decanoyl-Arg-Val-Lys-Arg chloromethylketone;HY-107760;CS-0029492;decanoyl-Arg-Val-Lys-Arg-chloromethyl-ketone;decanoyl-L-Arg-L-Val-L-Lys-L-Arg-chloromethylketone;Decanoyl-Arg-Val-Lys-Arg-chloromethylketonetrifluoroacetatesalt;N(2)-(1-oxodecyl)-L-arginyl-L-valyl-N-[(1S)-4-[(aminoiminomethyl)amino]-1-(2-chloroacetyl)butyl]-L-lysinamide;N(2)-decanoyl-L-arginyl-L-valyl-N-[(3S)-6-carbamimidamido-1-chloro-2-oxohexan-3-yl]-L-lysinamide;
Decanoyl-Arg-Val-Lys-Arg-chloromethylketone is a synthetic peptide-based compound designed as a potent and selective inhibitor of serine proteases, particularly those involved in coagulation and inflammatory pathways. Structurally, it features a chloromethylketone reactive group, which enables covalent modification and irreversible inhibition of target enzymes. The inclusion of a decanoyl moiety enhances its membrane permeability and biochemical stability, making it a valuable tool for probing protease function in complex biological systems. Its sequence specificity and irreversible binding mechanism have established it as a critical reagent in mechanistic studies of proteolytic enzymes and the regulation of protease-mediated signaling cascades.
Enzyme inhibition studies: As a chloromethylketone-derivatized tetrapeptide, this compound is widely employed in the characterization and functional dissection of serine proteases, including those implicated in coagulation, fibrinolysis, and inflammation. By covalently modifying the active site serine residue, it enables researchers to dissect enzyme mechanisms, determine substrate specificity, and evaluate the functional consequences of protease inhibition in vitro. Its use facilitates the identification of protease roles in physiological and pathological processes, supporting the development of targeted inhibitors and advancing fundamental enzymology.
Protease activity assays: The compound serves as a standard irreversible inhibitor in a variety of biochemical assays designed to quantify serine protease activity. By providing a means to block enzymatic function, it allows for the establishment of assay baselines, validation of protease-specific substrates, and assessment of the efficacy of novel protease inhibitors. Its high specificity and robust inhibitory profile make it a preferred choice for use in kinetic studies, inhibitor screening platforms, and structure-activity relationship analyses.
Signal transduction research: Protease-mediated signaling events are central to numerous cellular processes, including apoptosis, inflammation, and hemostasis. The application of this inhibitor in cell-based and biochemical models enables the selective abrogation of protease-driven signaling pathways, allowing researchers to delineate the downstream effects of protease inhibition. This approach supports the elucidation of complex signaling networks and the identification of protease substrates and interacting partners, contributing to a deeper understanding of cellular regulation.
Peptide substrate validation: The structurally defined sequence of the inhibitor provides a template for validating the substrate preferences of target enzymes. By comparing the reactivity of the inhibitor with various proteases, researchers can map substrate recognition motifs and optimize peptide sequences for use in synthetic substrates or further inhibitor development. This capability is particularly valuable in the rational design of protease probes and the refinement of high-throughput screening assays.
Biochemical pathway analysis: The irreversible nature and sequence specificity of the compound make it a powerful tool for dissecting protease-dependent pathways in complex biological samples. Its application enables the selective blockade of target proteases in cell lysates, tissue extracts, or reconstituted systems, facilitating the study of protease contributions to pathway regulation, feedback mechanisms, and cross-talk with other enzymatic systems. This targeted approach enhances the resolution of pathway analysis and supports the identification of novel regulatory nodes within protease networks.
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