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A protein Pascal triangle has been constructed as new type of supramolecular architecture by using the inducing ligand strategy that we previously developed for protein assemblies. Although mathematical studies on this famous geometry have a long history, no work on such Pascal triangles fabricated from native proteins has been reported so far due to their structural complexity. In this work, by carefully tuning the specific interactions between the native protein building block WGA and the inducing ligand R‐SL, a 2D Pascal‐triangle lattice with three types of triangular voids has been assembled. Moreover, a 3D crystal structure was obtained based on the 2D Pascal triangles. The distinctive carbohydrate binding sites of WGA and the intralayer as well as interlayer dimerization of RhB was the key to facilitate nanofabrication in solution. This strategy may be applied to prepare and explore various sophisticated assemblies based on native proteins. [ABSTRACT FROM AUTHOR]

A biomimetic conical submicrochannel (tip side ca. 400 nm) with functions of continuously tunable ion rectification and conductance based on thermoresponsive polymer layer‐by‐layer (LbL) self‐assembly is presented. These self‐assembled polymers with different layers exhibited a capability to regulate the effective channel diameter, and different ion rectifications/conductance were achieved. By controlling temperature, the conformation and wettability of the assembled polymers were reversibly transformed, thus the ion rectification/conductance could be further adjusted subtly. Owing to the synergistic effect, the ion conductance could be tuned over a wide range spanning three orders of magnitude. Moreover, the proposed system can be applied for on‐demand on‐off molecule delivery, which was important for disease therapy. This study opens a new door for regulating channel size according to actual demand and sensing big targets with different size with one channel. [ABSTRACT FROM AUTHOR]

In nature, proteins self-assemble into various structures with different dimensions. To construct these nanostructures in laboratories, normally proteins with different symmetries are selected. However, most of these approaches are engineering-intensive and highly dependent on the accuracy of the protein design. Herein, we report that a simple native protein LecA assembles into one-dimensional nanoribbons and nanowires, two-dimensional nanosheets, and three-dimensional layered structures controlled mainly by small-molecule assembly-inducing ligands RnG ( n=1, 2, 3, 4, 5) with varying numbers of ethylene oxide repeating units. To understand the formation mechanism of the different morphologies controlled by the small-molecule structure, molecular simulations were performed from microscopic and mesoscopic view, which presented a clear relationship between the molecular structure of the ligands and the assembled patterns. These results introduce an easy strategy to control the assembly structure and dimension, which could shed light on controlled protein assembly. [ABSTRACT FROM AUTHOR]

In nature, proteins are organized into highly ordered self‐assembled structures with various morphologies and dimensions. In their Communication on page 10691 ff., Y. Ma, G. Chen, and co‐workers report the fabrication of protein assemblies by using native protein LecA as a building block through sugar‐‐protein interactions and rhodamine dimerization. The morphologies and dimensions of the protein assemblies can be controlled by the length of the tether between the sugar and rhodamine. [ABSTRACT FROM AUTHOR]