3 years ago

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

Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
Yan Lu, Zdravko Kochovski, Ming Jiang, Yu-qiang Ma, Guosong Chen, Guang Yang, Rongting Hu, Hong-ming Ding
In nature, proteins are organized into highly ordered self-assembled structures with various morphologies and dimensions. In their Communication (DOI: 10.1002/anie.201703052), 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.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201707041

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