Highly Ordered Self‐Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly‐Inducing Ligands

Abstract

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.

On-Axis Alignment of Protein Nanocage Assemblies from 2D to 3D through the Aromatic Stacking Interactions of Amino Acid Residues

“…These are (1) the matching rotational symmetry approach, 9,11,17 (2) computational optimization of protein−protein interfaces, 18,19 (3) disulfide bonds or metal ions to coordinate proteins, 14,20,21 and (4) the use of bifunctional ligands. 22,23 However, these approaches are usually engineering-intensive and highly dependent on the accuracy of the design; the extensive reengineering and modification of protein surface that is usually required to construct the interfaces may negatively impact the biological activity of the designed protein. Despite great progress, the design of protein systems that assemble into well-defined architectures remains a challenging goal.…”

Controlling the Interaction of Nanoparticles with Cell Membranes by the Polymeric Tether

“…Notably, the linked nanoparticles modeled here have not been reported previously. Nevertheless, there were many approaches (like DNA hybridization, 34,35 π−π stacking/lectin−sugar interaction, 36 and disulfides 37 ) to link/cross-link the nanoparticles/biomolecules in supramolecular field, which may be utilized to synthetize the linked nanoparticles. For example, when the concentration of the nanoparticles (dendrimers) and disulfides was very low in the experiment, 37 the linked nanoparticles via one or two chains (instead of cross-linked multiple nanoparticles) may be formed.…”

Competition between Supramolecular Interaction and Protein–Protein Interaction in Protein Crystallization: Effects of Crystallization Method and Small Molecular Bridge

“…R1M, R2M, and R5M were synthesized according to our previous synthesis protocols (Figure S1). 10,17 The synthesis scheme of RnM (n = 1−5) is shown in Figure S1. R3M and R4M were synthesized according to our previous literature.…”