Despite the tremendous efforts devoted to the structural analysis of hydrogel microspheres (microgels), many details of their structures remain unclear. Reported in this study is that thermoresponsive poly(N‐isopropyl acrylamide) (pNIPAm)‐based microgels exhibit not only the widely accepted core–shell structures, but also inhomogeneous decanano‐sized non‐thermoresponsive spherical domains within their dense cores, which was revealed by temperature‐controlled high‐speed atomic force microscopy (TC‐HS‐AFM). Based on a series of experiments, it is concluded that the non‐thermoresponsive domains are characteristic for pNIPAm microgels synthesized by precipitation polymerization, and plausible structures for microgels prepared by other polymerization techniques are proposed.

Porous molecular cages have a characteristic processability arising from their solubility, which allows their incorporation into porous materials. Attaining solubility often requires covalently bound functional groups that are unnecessary for porosity and which ultimately occupy free volume in the materials, decreasing their surface areas. Here, a method is described that takes advantage of the coordination bonds in metal–organic polyhedra (MOPs) to render insoluble MOPs soluble by reversibly attaching an alkyl‐functionalized ligand. We then use the newly soluble MOPs as monomers for supramolecular polymerization reactions, obtaining permanently porous, amorphous polymers with the shape of colloids and gels, which display increased gas uptake in comparison with materials made with covalently functionalized MOPs.

Non-enzymatic proteins including antibodies function as biomarkers and are used as biopharmaceuticals in several diseases. Protein-responsive soft materials capable of the controlled release of drugs and proteins have potential for use in next-generation diagnosis and therapies. Here, we describe a supramolecular/agarose hydrogel composite that can release a protein in response to a non-enzymatic protein. A non-enzymatic protein-responsive system is developed by hybridization of an enzyme-sensitive supramolecular hydrogel with a protein-triggered enzyme activation set. In situ imaging shows that the supramolecular/ agarose hydrogel composite consists of orthogonal domains of supramolecular fibers and agarose, which play distinct roles in protein entrapment and mechanical stiffness, respectively. Integrating the enzyme activation set with the composite allows for controlled release of the embedded RNase in response to an antibody. Such composite hydrogels would be promising as a matrix embedded in a body, which can autonomously release biopharmaceuticals by sensing biomarker proteins.

Time-resolved dynamic light scattering unveiled the multiscale self-assembly mechanism of metal–organic polyhedra and allowed for inducing asymmetry in a porous gel.

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