Effects of the crystallization temperature on the crystal structure and its melting behavior of poly (l-lactic acid) (PLLA) have been investigated by means of wide-angle (WAXS) and small-angle (SAXS) X-ray scattering, optical microscopy, and differential scanning calorimetory (DSC). PLLA was found to crystallize as the α form when the crystallization temperature T c was higher than 120 °C, while significant change in lattice parameters was seen for T c's below 120 °C. The ratio of the a- and b-axis lengths begins to decrease with T c below 120 °C and is 31/2 below 90 °C, which suggests a new crystalline form with hexagonal packing, namely, the α‘ form. The possible reason for α‘ formation is discussed. High-temperature WAXS and SAXS measurements showed that α‘ crystal transforms into ordered a form during heating. The transition takes place at 150 °C without a decrease in scattering intensity and without heating rate dependence. The mechanism for the transition is discussed.
Effects of the addition of PDLA on the crystallization behavior of PLLA was investigated by means of differential scanning calorimetry, wide-angle X-ray diffraction, melt rheology, and polarized optical microscopy. Nonisothermal and isothermal crystallization behavior of PLLA including low (l-PDLA) and high molecular weight PDLA (h-PDLA) were studied. PLLA/PDLA asymmetric blends form stereocomplex (SC) crystal and stay unmelted at 200 °C in the PLLA melt. Nonisothermal crystallization measurement from 200 °C showed monotonous rise in the crystallization temperature for PLLA/h-PDLA blend, while peculiar concentration dependence was observed for PLLA/l-PDLA blends. The acceleration effect was more pronounced in PLLA/h-PDLA, although the crystallinity of SC was lower than PLLA/l-PDLA blends, which implies the importance of higher order structure of SC for the crystallization of PLLA. From isothermal crystallization kinetics measurements, the acceleration effect in PLLA/h-and l-PDLA blends was found to enhance the nucleation of crystallization but slightly interrupts the crystallization growth. The above results were reasonably explained by the model where SC crystallites are not isolated in PLLA melt but connected like a physical gel.
Polycomb repressive complex 2 (PRC2) methylates histone H3 lysine 27 and represses gene expression to regulate cell proliferation and differentiation. Enhancer of zeste homolog 2 (EZH2) or its close homolog EZH1 functions as a catalytic subunit of PRC2, so there are two PRC2 complexes containing either EZH2 or EZH1. Tumorigenic functions of EZH2 and its synthetic lethality with some subunits of SWItch/Sucrose Non‐Fermentable (SWI/SNF) chromatin remodeling complexes have been observed. However, little is known about the function of EZH1 in tumorigenesis. Herein, we developed novel, orally bioavailable EZH1/2 dual inhibitors that strongly and selectively inhibited methyltransferase activity of both EZH2 and EZH1. EZH1/2 dual inhibitors suppressed trimethylation of histone H3 lysine 27 in cells more than EZH2 selective inhibitors. They also showed greater antitumor efficacy than EZH2 selective inhibitor in vitro and in vivo against diffuse large B‐cell lymphoma cells harboring gain‐of‐function mutation in EZH2. A hematological cancer panel assay indicated that EZH1/2 dual inhibitor has efficacy against some lymphomas, multiple myeloma, and leukemia with fusion genes such as MLL‐AF9,MLL‐AF4, and AML1‐ETO. A solid cancer panel assay demonstrated that some cancer cell lines are sensitive to EZH1/2 dual inhibitor in vitro and in vivo. No clear correlation was detected between sensitivity to EZH1/2 dual inhibitor and SWI/SNF mutations, with a few exceptions. Severe toxicity was not seen in rats treated with EZH1/2 dual inhibitor for 14 days at drug levels higher than those used in the antitumor study. Our results indicate the possibility of EZH1/2 dual inhibitors for clinical applications.
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