15 research outputs found

    Passivation properties and formation mechanism of amorphous halide perovskite thin films

    Get PDF
    Lead halide perovskites are among the most exciting classes of optoelectronic materials due to their unique ability to form high‐quality crystals with tunable bandgaps in the visible and near‐infrared using simple solution precipitation reactions. This facile crystallization is driven by their ionic nature; just as with other salts, it is challenging to form amorphous halide perovskites, particularly in thin‐film form where they can most easily be studied. Here, rapid desolvation promoted by the addition of acetate precursors is shown as a general method for making amorphous lead halide perovskite films with a wide variety of compositions, including those using common organic cations (methylammonium and formamidinium) and anions (bromide and iodide). By controlling the amount of acetate, it is possible to tune from fully crystalline to fully amorphous films, with an interesting intermediate state consisting of crystalline islands embedded in an amorphous matrix. The amorphous lead halide perovskite has a large and tunable optical bandgap. It improves the photoluminescence quantum yield and lifetime of incorporated crystalline perovskite, opening up the intriguing possibility of using amorphous perovskite as a passivating contact, as is currently done in record efficiency silicon solar cells

    Identification of an acetylation-dependant Ku70/FLIP complex that regulates FLIP expression and HDAC inhibitor-induced apoptosis

    No full text
    FLIP is a potential anti-cancer therapeutic target that inhibits apoptosis by blocking caspase 8 activation by death receptors. We report a novel interaction between FLIP and the DNA repair protein Ku70 that regulates FLIP protein stability by inhibiting its polyubiquitination. Furthermore, we found that the histone deacetylase (HDAC) inhibitor Vorinostat (SAHA) enhances the acetylation of Ku70, thereby disrupting the FLIP/Ku70 complex and triggering FLIP polyubiquitination and degradation by the proteasome. Using in vitro and in vivo colorectal cancer models, we further demonstrated that SAHA-induced apoptosis is dependant on FLIP downregulation and caspase 8 activation. In addition, an HDAC6-specific inhibitor Tubacin recapitulated the effects of SAHA, suggesting that HDAC6 is a key regulator of Ku70 acetylation and FLIP protein stability. Thus, HDAC inhibitors with anti-HDAC6 activity act as efficient post-transcriptional suppressors of FLIP expression and may, therefore, effectively act as ‘FLIP inhibitors'
    corecore