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  • Identification and characterization of the novel reversible and selective cathepsin X inhibitors [Elektronski vir]
    Pečar Fonović, Urša ...
    Cathepsin X is a cysteine peptidase involved in the progression of cancer and neurodegenerative diseases. Targeting this enzyme with selective inhibitors opens a new possibility for intervention in ... several therapeutic areas. In this study triazole-based reversible and selective inhibitors of cathepsin X have been identified. Their selectivity and binding is enhanced when the 2,3-dihydrobenzo[b][1,4]dioxine moiety is present as the R1 substituent. Of a series of selected triazole-benzodioxine derivatives, compound 22 is the most potent inhibitor of cathepsin X carboxypeptidase activity (Ki%=%2.45%%%0.05 microM) with at least 100-fold greater selectivity in comparison to cathepsin B or other related cysteine peptidases. Compound 22 is not cytotoxic to prostate cancer cells PC-3 or pheochromocytoma PC-12 cells at concentrations up to 10% microM. It significantly inhibits the migration of tumor cells and increases the outgrowth of neurites, both processes being under the control of cathepsin X carboxypeptidase activity. Compound 22 and other characterized triazole-based inhibitors thus possess a great potential for further development resulting in several in vivo applications.
    Source: Scientific reports [Elektronski vir]. - ISSN 2045-2322 (Vol. 7, art. no. 11459, 2017, str. 1-11)
    Type of material - e-article
    Publish date - 2017
    Language - english
    COBISS.SI-ID - 4382065

    Link(s):

    https://www.nature.com/articles/s41598-017-11935-1
    DOI

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