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Recent progress in ring-opening (co)polymerization of γ-butyrolactone (γBL) in the presence of various initiating/catalyst systems has been reviewed. Low reaction temperatures and high monomer concentrations are critical for the success of such polymerization, regardless of the different initiating/catalyst systems.
Water desalination through a reverse osmosis (RO) membrane is an important technology for producing pure water from seawater. High-performance membrane materials have been extensively developed because these materials are useful as core elements in practical water separation processes. Bridged polysilsesquioxane (PSQ)-derived membranes are promising candidates for robust RO membranes because they exhibit high thermal stability and chlorine resistance compared to conventional aromatic polyamide membranes. This review reports on our recent studies involving the development of RO membranes based on bridged PSQs.
There is increasing interest in solid particle-stabilized soft dispersed systems, including bubbles/foams (a gas-in-liquid dispersed system) and liquid marbles (a liquid-in-gas dispersed system). Synthetic colloidal polymer particles are attractive stabilizers, as their hydrophilic–hydrophobic character and surface chemistries can be designed and controlled on demand via polymerization with various functional monomers and post polymer reactions. In this review article, bubbles/foams and liquid marbles stabilized solely with stimulus-responsive polymer particles will be reviewed. The stabilities, structures, and motions of these dispersed systems can be controlled by external stimuli.
The cationic comb-type copolymers, which consisted of a polycation backbone grafted with high density of hydrophilic chains, form soluble and soft interpolyelectrolyte complexes with biopolymers and act as an artificial chaperone to assist in the folding of nucleic acids and peptides. The copolymers stabilize DNA duplex, triplex, and quadruplex structures and accelerate strand exchange reactions as well as assist in the folding of functional peptides into the active conformation.
