The polymerization-induced self-assembly (PISA) has been developed with great success and rapidly promoted the application of the self-assembly technique in practice. The living anionic polymerization (LAP) is represented as a paragon in polymer chemistry because of its versatility in the synthesis of well-defined model polymers with many advantages. However, the combination of the LAP mechanism with the PISA process is still rarely succeeded and remains a challenge. In this contribution, the LAP PISA was realized by using diblock copolymer polyisoprene-b-polystyrene (PI-b-PS) as a research model. The comprehensive variation of the factors, such as the molecular weights (MWs) of PI and PS segments, targeted MW ratio M n,PS /M n,PI , weight solid content, and kinds of comonomers, provided an efficient way to modulate the morphologies. The generated nano-objects included the spherical, wormlike, vesicular micelles, as well as their mixtures. Uniquely, based on the in-situ, site-specific cross-linking of the living species in the final polymerization stage of the LAP PISA process, the generated nano-objects can selectively and efficiently be stabilized by a divinylbenzene agent.

Dual stimuli-responsive unimolecular micelles from “Y”-shape armed amphiphilic star-like copolymer are designed for controlled drug delivery.

Nanopipettes provide a promising confined space that enables advances in single-molecule analysis, and their unique conical tubular structure is also suitable for single-cell analysis. In this work, functionalized-nanopore-based single-entity electrochemistry (SEE) analysis tools were developed for the label-free monitoring of single-molecule glycoprotein−boronate affinity interaction for the first time, and immunoglobulin G (IgG, one of the important biomarkers for many diseases such as COVID-19 and cancers) was employed as the model glycoprotein. The principle of this method is based on a single glycoprotein molecule passing through 4-mercaptophenylboronic acid (4-MPBA)-modified nanopipettes under a bias voltage and in the meantime interacting with the boronate group from modified 4-MPBA. This translocation and affinity interaction process can generate distinguishable current blockade signals. Based on the statistical analysis of these signals, the equilibrium association constant (κ a ) of single-molecule glycoprotein−boronate affinity interaction was obtained. The results show that the κ a of IgG in the confined nanopore at the single-molecule level is much larger than that measured in the open system at the ensemble level, which is possibly due to the enhanced multivalent synergistic binding in the restricted space. Moreover, the functionalized-nanopore-based SEE analysis tools were further applied for the label-free detection of IgG, and the results indicate that our method has potential application value for the detection of glycoproteins in real samples, which also paves way for the single-cell analysis of glycoproteins.

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