150113-99-8

Usage

Uses

Used in Pharmaceutical Industry:
DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE is used as a therapeutic agent for the inhibition of the Chikungunya virus (CHIKV). This mosquito-transmitted Alphavirus causes acute infection in humans, characterized by symptoms such as polyarthralgia, fever, myalgia, and headache. By inhibiting the Furin enzyme, which plays a crucial role in the viral replication process, DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE can potentially limit the spread and severity of the Chikungunya virus.
Additionally, Furin inhibitors like DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE may have broader applications in the treatment of other viral infections and diseases where the Furin enzyme is involved in their pathogenesis. Further research and development in this area could lead to the discovery of new therapeutic strategies against a range of diseases.

Biological Activity

decanoyl-rvkr-cmk is a proprotein convertase inhibitor [1].proprotein convertases (pcs) are involved in generating bioactive peptides, as well as activating several enzymes and growth factors in many important physiological events. pcs play important roles in several pathologies including viral infections and cancers. thus, pcs are promising targets for therapeutic applications [1].in pc12 cells, the pc enzyme inhibitor decanoyl-rvkr-cmk at ~ 100 μm, resulted in partial block of regulated vgf release at 48 h and a complete block at 96 h, without significant change in basal vgf release. also, decreased vgf processing was observed in cell extracts and media from decanoyl-rvkr-cmk-treated pc12 cultures [2].in k5-pace4 transgenic mice topically treated with the hyperplasiogenic phorbol ester 12-o-tetradecanoylphorbol-13-acetate (tpa), a 2-day topical treatment of decanoyl-rvkr-cmk at 300 μm, inhibited tpa-induced epidermal proliferation. when decanoyl-rvkr-cmk treatment (100 μm, q.d.) was extended for 3 weeks, decreasing numbers of ki-67-labeled cells were shown in both k5-pace4 mice epidermal basal epidermal keratinocytes and wild-type mouse epidermis [3].[1]. fugère m, day r. cutting back on pro-protein convertases: the latest approaches to pharmacological inhibition. trends in pharmacological sciences, 2005, 26(6): 294-301.[2]. garcia a l, han s k, janssen w g, et al. a prohormone convertase cleavage site within a predicted alpha-helix mediates sorting of the neuronal and endocrine polypeptide vgf into the regulated secretory pathway. journal of biological chemistry, 2005, 280(50): 41595-41608.[3]. bassi d e, zhang j, cenna j, et al. proprotein convertase inhibition results in decreased skin cell proliferation, tumorigenesis, and metastasis. neoplasia, 2010, 12(7): 516-526.