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

Angewandte Chemie
Guang YangMing Jiang

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.

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Citations

Feb 16, 2018·Physical Chemistry Chemical Physics : PCCP·You-Sheng YuYu-Qiang Ma
Aug 2, 2018·Angewandte Chemie·Norifumi KawakamiKenji Miyamoto
Nov 20, 2018·Chemical Society Reviews·Seah Ling KuanTanja Weil
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Mar 10, 2020·Angewandte Chemie·Rongying LiuMing Jiang
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May 13, 2021·Biomacromolecules·Shengwang ZhouMilan Mrksich
Mar 17, 2020·Accounts of Chemical Research·Chendi Gao, Guosong Chen
Aug 19, 2021·Chemical Reviews·Jie ZhuF Akif Tezcan
Sep 3, 2019·Langmuir : the ACS Journal of Surfaces and Colloids·Song-di NiYu-Qiang Ma
Mar 27, 2019·Biomacromolecules·Ian W Hamley

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