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Summary of main observation and conclusion: In recent years, synthesis of hybrid heteroarm star polymer with precisely defined arms has evolved to be one of the most attractive topics within polymer chemistry. In this study, we present the successful synthesis of metallacycle‐linked heteroarm star polymers (HASPs) composed of crystalline poly(ε‐caprolactone) (PCL) and polyacrylate (poly (N‐isopropylacrylamide) (PNIPAM) segments via combination of ring‐opening polymerization (ROP) and reversible addition‐fragmentation chain transfer (RAFT) controlled radical polymerization. Firstly, a hexagonal metallacycle containing three hydroxy groups and three chain transfer agent moieties at the alternative vertexes was designed and synthesized based on the general principle of coordination‐driven self‐assembly. Subsequently, upon combination of two orthogonal post‐assembly polymerizations, a new family of HASPs containing a well‐defined hexagonal metallacycle with precisely controlled position of polymer arms was facilely prepared. Interestingly, the obtained HASPs could spontaneously self‐assemble into large‐area and regular cubic nanoparticles in tetrahydrofuran (THF)/methanol (MeOH) mixed solvents under specific conditions as confirmed by scanning electron microscopy (SEM) and atomic force microscopy (AFM). This study provides a simple route to the controllable preparation of HASPs, and opens up a new way for further study on self‐assembly of different HASPs systems. [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 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]