The potential of hydrogen hydrate as a future hydrogen storage medium.

Hydrogen is recognized as the "future fuel" and the most promising alternative of fossil fuels due to its remarkable properties including exceptionally high energy content per unit mass (142 M J / k g ), low mass density, and massive environmental and economical upsides. A wide spectrum of methods in H 2 production, especially carbon-free approaches, H 2 purification, and H 2 storage have been investigated to bring this energy source closer to the technological deployment. Hydrogen hydrates are among the most intriguing material paradigms for H 2 storage due to their appealing properties such as low energy consumption for charge and discharge, safety, cost-effectiveness, and favorable environmental features. Here, we comprehensively discuss the progress in understanding of hydrogen clathrate hydrates with an emphasis on charging/discharging rate of H 2 (i.e. hydrate formation and dissociation rates) and the storage capacity. A thorough understanding on phase equilibrium of the hydrates and its variation through different materials is provided. The path toward ambient temperature and pressure hydrogen batteries with high storage capacity is elucidated. We suggest that the charging rate of H 2 in this storage medium and long cyclic performance are more immediate challenges than storage capacity for technological translation of this storage medium. This review and provided outlook establish a groundwork for further innovation on hydrogen hydrate systems for promising future of hydrogen fuel.

PASylation Enhances the Stability, Potency, and Plasma Half-Life of Interferon α-2a: A Molecular Dynamics Simulation.

In this study, the effectiveness of PASylation in enhancing the potency and plasma half-life of pharmaceutical proteins has been accredited as an alternative technique to the conventional methods such as PEGylation. Proline, alanine, and serine (PAS) chain has shown some advantages including biodegradability improvement and plasma half-life enhancement while lacking immunogenicity or toxicity. Although some experimental studies have been performed to find the mechanism behind PASylation, the detailed mechanism of PAS effects on the pharmaceutical proteins has remained obscure, especially at the molecular level. In this study, the interaction of interferon α-2a (IFN) and PAS chain is investigated using molecular dynamics simulation method. Several important parameters including secondary structure, root-mean-square distance, and solvent accessible surface area to investigate the stability, bioavailability, and bioactivity of the PASylated protein are studied. The results demonstrate that IFN conformation is not affected critically through PASylation while it results in improvement of the protein stability and bioactivity. Therefore, PASylation can be considered as a proper biological alternative technique to increase the plasma half-life of the biopharmaceutical proteins through enlarging apparent volume. The proposed simulation represents a computational approach that would provide a basis for the study of PASylated pharmaceutical proteins for different future applications.