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Anion transmembrane nanochannels constructed from dynamic covalent helices (DCHs) are reported. The dynamic covalent structures can be synthesized by one-pot dynamic covalent reactions and helically self-fold into nanotubes through intramolecular hydrogen bonding and π-π interactions. Such helical structures can vertically self-assemble into long nanofibers under π-π stacking and their hollow nanocavities finally form ion permeation pathways across the lipid membranes. Single-channel electrophysiology signals provide solid evidence of DCHs following the channel rather than the carrier mechanism. Owing to the pore-forming capacity of DCHs, nanochannels are able to accelerate the movement of anions across lipid membranes with high transport activity (EC50 =0.08 mol %). Moreover, DCH channels show dehydration energy dependent anion selectivity. This report highlights the importance of such DCHs as general channel scaffolds with economical synthesis and special nanocavities.

An effective method is reported to synthesize aromatic helical polymer nanochannels by combining both the well-studied aromatic amide helical codons with pyridine-oxadiazole helical codons into helical structure sequences. With this strategy, a type of helical polymer nanochannel that shows structure-directed transmembrane transport functions is synthesized. Although such nanochannels show relatively weak selectivity for the transportation of alkali metal ions, accessible chemical mutation of helical structure sequences will provide a great chance for the design of desired channel property. The straightforward preparation of well-established pyridine-oxadiazole helical structure will significantly promote the synthesis of this kind of aromatic helical polymer nanochannels. With the development of aromatic amide foldamers, moreover, a number of "monomers" will be available for the preparation of helical polymer nanochannels.

A tellurium-based polymeric sufactant as a selen-enzyme model has been constructed by employing 11-acryl-oyloxyundecyltriethylammonium bromide (AUTEAB, 4) and a tellurium-containing compound (1). It demonstrates strong substrate binding ability for thiols and high glutathione peroxidase (GPx) activity about 6 orders of magnitude more efficient than the well-known GPx mimic PhSeSePh in an ArSH assay system. More importantly. a series of telhirium-based polymeric micelle catalysts with the catalytic tellurium center located at various positions in the micelle have been constructed, and the dramatic difference in activity indicates that the exact match of the catalytic center and binding site plays a key role in enzyme catalytic efficiency.