TY  - JOUR
A1  - Yang, Guang
A1  - Ding, Hong-ming
A1  - Kochovski, Zdravko
A1  - Hu, Rongting
A1  - Lu, Yan
A1  - Ma, Yu-qiang
A1  - Chen, Guosong
A1  - Jiang, Ming
T1  - Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
JF  - Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition
N2  - 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.
KW  - carbohydrate-protein interactions
KW  - dual non-covalent interactions
KW  - molecular simulations
KW  - protein self-assembly
Y1  - 2017
U6  - https://doi.org/10.1002/anie.201703052
SN  - 1433-7851
SN  - 1521-3773
VL  - 56
SP  - 10691
EP  - 10695
PB  - Wiley-VCH
CY  - Weinheim
ER  -