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Highly Ordered Self‐Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly‐Inducing Ligands
Author(s) -
Yang Guang,
Ding Hongming,
Kochovski Zdravko,
Hu Rongting,
Lu Yan,
Ma Yuqiang,
Chen Guosong,
Jiang Ming
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201703052
Subject(s) - self assembly , mesoscopic physics , nanotechnology , molecule , nanowire , materials science , nanostructure , chemistry , physics , organic chemistry , quantum mechanics
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.