Investigation of the conformation of human prion protein in ethanol solution using molecular dynamics simulations.

When the conformation of protein is changed from its natural state to a misfolded state, some diseases will happen like prion disease. Prion diseases are a set of deadly neurodegenerative diseases caused by prion protein misfolding and aggregation. Monohydric alcohols have a strong influence on the structure of protein. However, whether monohydric alcohols inhibit amyloid fibrosis remains uncertain. Here, to elucidate the effect of ethanol on the structural stability of human prion protein, molecular dynamics simulations were employed to analyze the conformational changes and dynamics characteristics of human prion proteins at different temperatures. The results show that the extension of ß-sheet occurs more easily and the α-helix is more easily disrupted at high temperatures. We found that ethanol can destroy the hydrophobic interactions and make the hydrogen bonds stable, which protects the secondary structure of the protein, especially at 500 K.Communicated by Ramaswamy H. Sarma.

Junctionless Thin-Film Transistors Gated by an H3PO4-Incorporated Chitosan Proton Conductor.

We fabricated an H3PO4-incorporated chitosan proton conductor film that exhibited the electric double layer effect and showed a high specific capacitance of 4.42 µF/cm2. Transparent indium tin oxide thin-film transistors gated by H3PO4-incorporated chitosan films were fabricated by sputtering through a shadow mask. The operating voltage was as low as 1.2 V because of the high specific capacitance of the H3PO4-incorporated chitosan dielectrics. The junctionless transparent indium tin oxide thin film transistors exhibited good performance, including an estimated current on/off ratio and field-effect mobility of 1.2 × 106 and 6.63 cm2V-1s-1, respectively. These low-voltage thin-film electric-double-layer transistors gated by H3PO4-incorporated chitosan are promising for next generation battery-powered "see-through" portable sensors.