Busan port's development into a Northeast Asian hub-port & 「the Korea-Japan strait economic Bloc」

노트 : 2008 Proceedings of The 6th International Joint Conferenc

Nanoseeded Catalytic Terpolymerization of CO, Ethylene, and Propylene by Size-Controlled SiO₂@Sulfonated Microporous Organic Polymer

Nanoseeds with silica@sulfonated microporous organic polymer (SiO₂@S-MOP) structure were prepared by the formation of MOP layers on the surface of SiO₂ spheres and the successive sulfonation of the MOPs. Using the SiO₂@S-MOPs as seed materials, catalytic terpolymerization of CO, ethylene, and propylene was studied. The designed SiO₂@S-MOP nanoseeds not only activated catalyst precursors but also controlled the catalytic formation of polyketones. While the homogeneous system showed a severe reactor fouling and a wide molecular weight distribution of terpolymer, the SiO₂-190@S-MOP system resulted in the narrow molecular weight distribution of terpolymers without a reactor fouling. The size of nanoseeds was critical to obtaining the granular terpolymers. Moreover, the SiO₂-190@S-MOP system showed a good activity of 17.2 kg of polymer/g of Pd, comparable to the homogeneous system with 19.6 kg of polymer/g of Pd. We believe that more various nanoseeded catalytic polymerizations can be developed using new nanoseed materials adopting the MOP chemistry

Long-chain polyphosphates impair SARS-CoV-2 infection and replication

Inorganic polyphosphates (polyPs) are linear polymers composed of repeated phosphate (PO4 3-) units linked together by multiple high-energy phosphoanhydride bonds. In addition to being a source of energy, polyPs have cytoprotective and antiviral activities. Here, we investigated the antiviral activities of long-chain polyPs against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. In molecular docking analyses, polyPs interacted with several conserved amino acid residues in angiotensin-converting enzyme 2 (ACE2), the host receptor that facilitates virus entry, and in viral RNA-dependent RNA polymerase (RdRp). ELISA and limited proteolysis assays using nano- LC-MS/MS mapped polyP120 binding to ACE2, and site-directed mutagenesis confirmed interactions between ACE2 and SARS-CoV-2 RdRp and identified the specific amino acid residues involved. PolyP120 enhanced the proteasomal degradation of both ACE2 and RdRp, thus impairing replication of the British B.1.1.7 SARS-CoV-2 variant. We thus tested polyPs for functional interactions with the virus in SARS-CoV-2-infected Vero E6 and Caco2 cells and in primary human nasal epithelial cells. Delivery of a nebulized form of polyP120 reduced the amounts of viral positive-sense genomic and subgenomic RNAs, of RNA transcripts encoding proinflammatory cytokines, and of viral structural proteins, thereby presenting SARS-CoV-2 infection in cells in vitro