Lithium metal oxide nanoparticles were synthesized by induction thermal plasma. Four different systems—Li–Mn, Li–Cr, Li–Co, and Li–Ni—were compared to understand formation mechanism of Li–Me oxide nanoparticles in thermal plasma process. Analyses of X-ray diffractometry and electron microscopy showed that Li–Me oxide nanoparticles were successfully synthesized in Li–Mn, Li–Cr, and Li–Co systems. Spinel structured LiMn2O4 with truncated octahedral shape was formed. Layer structured LiCrO2 or LiCoO2 nanoparticles with polyhedral shapes were also synthesized in Li–Cr or Li–Co systems. By contrast, Li–Ni oxide nanoparticles were not synthesized in the Li–Ni system. Nucleation temperatures of each metal in the considered system were evaluated. The relationship between the nucleation temperature and melting and boiling points suggests that the melting points of metal oxides have a strong influence on the formation of lithium metal oxide nanoparticles. A lower melting temperature leads to a longer reaction time, resulting in a higher fraction of the lithium metal oxide nanoparticles in the prepared nanoparticles.
The binding process of angiotensin-converting enzyme 2 (ACE2) to the receptor-binding
domain (RBD) of the severe acute respiratory syndrome-like coronavirus 2 spike protein
was investigated using molecular dynamics simulation and the three-dimensional reference
interaction-site model theory. The results suggested that the protein-binding process
consists of a protein–protein approaching step, followed by a local structural
rearrangement step. In the approaching step, the interprotein interaction energy
decreased as the proteins approached each other, whereas the solvation free energy
increased. As the proteins approached, the glycan of ACE2 first established a hydrogen
bond with the RBD. Thereafter, the number of interprotein hydrogen bonds increased
rapidly. The solvation free energy increased because of the desolvation of the protein
as it approached its partner. The spatial distribution function of the solvent revealed
the presence of hydrogen bonds bridged by water molecules on the RBD–ACE2
interface. Finally, principal component analysis revealed that ACE2 showed a pronounced
conformational change, whereas there was no significant change in RBD.
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