ARID1A regulates expression of SOX9, activation of the mTOR pathway, and differentiation of PDCs. ARID1A inhibits formation of PDACs from IPMNs in mice with pancreatic expression of activated KRAS and is down-regulated in IPMN and PDAC tissues from patients.
Global ecological damage has heightened the demand for silk as ‘a structural material made from sustainable resources’. Scientists have earnestly searched for stronger and tougher silks. Bagworm silk might be a promising candidate considering its superior capacity to dangle a heavy weight, summed up by the weights of the larva and its house. However, detailed mechanical and structural studies on bagworm silks have been lacking. Herein, we show the superior potential of the silk produced by Japan’s largest bagworm,
Eumeta variegata
. This bagworm silk is extraordinarily strong and tough, and its tensile deformation behaviour is quite elastic. The outstanding mechanical property is the result of a highly ordered hierarchical structure, which remains unchanged until fracture. Our findings demonstrate how the hierarchical structure of silk proteins plays an important role in the mechanical property of silk fibres.
Crystallization behavior of palm oil and tripalmitin (PPP) in a model margarine system was investigated. The model margarine was held in a programmable oven, heated to 5°C for 12 h and then 20°C for a further 12 h. After 3 weeks, the model margarine was evaluated by polarization microscopy. Granular crystals were observed in the margarine containing an excess amount of palm oil and PPP. The concentration of higher-melting fatty acids was higher in the crystals relative to the surroundings. Likewise, the presence of lower-melting fatty acids was lower in the crystals. The polymorphic structure of the margarine with excess palm oil and PPP was determined to be all b¢ by X-RD spectra. The result suggested that the agglomeration of higher-melting point triglycerides (TAGs), such as PPP in this study, led to the formation of granular crystals in the margarine without b polymorphic emergence.
Enhancing the molecular orientation of the regenerated silk fibroin (RF) up to a level comparable to the native silk is highly challenging. Our novel and promising strategy for the poststretching process is (1) creating at first an α-helix-HFIP complex with a hexagonal packing as an intermediate state and then (2) stretching it at a high temperature to induce the helix-to-sheet structural phase transition. Here we show for the first time the significantly high stretching efficiency of the proposed technique compared with the conventional wet-stretching techniques and the successful achievement of higher crystalline orientation and higher Young's modulus compared even with the native silk. The detailed structural analysis based on the time-resolved simultaneous measurement of stress-strain curve, synchrotron X-ray scatterings, and FTIR has revealed the structural transition mechanism from the hexagonally packed α-helix-HFIP complex to the highly oriented β-sheet crystalline state as well as the critical level of crystal orientation needed for the helix-to-sheet transition.
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