![]() Received: AugAccepted: OctoPublished: November 12, 2015Ĭopyright: © 2015 Ramalho et al. (2015) Imaging Sites of Inhibition of Proteolysis in Pathomimetic Human Breast Cancer Cultures by Light-Activated Ruthenium Compound. We suggest that caged inhibitor 2 is a prototype for cathepsin B inhibitors that can control both the site and timing of inhibition in cancer.Ĭitation: Ramalho SD, Sharma R, White JK, Aggarwal N, Chalasani A, Sameni M, et al. Upon light activation, compound 2, like compound 1, inhibited cathepsin B activity and pericellular collagen IV degradation by the 3D pathomimetic models of living breast cancer cells, without causing toxicity. ![]() We further report the synthesis and characterization of a caged version of compound 1, (BF 4) 2 (compound 2), which can be photoactivated with visible light. To image, localize and quantify collagen IV degradation in real-time we used 3D pathomimetic breast cancer models designed to mimic the in vivo microenvironment of breast cancers. We demonstrate inhibition by a dipeptidyl nitrile inhibitor (compound 1) of cathepsin B activity and also of pericellular degradation of dye-quenched collagen IV by living breast cancer cells. ![]() The cysteine protease cathepsin B has been causally linked to progression and metastasis of breast cancers. ![]()
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