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 - TY - JOUR A1 - Yang, Guang A1 - Hu, Rongting A1 - Ding, Hong-ming A1 - Kochovski, Zdravko A1 - Mei, Shilin A1 - Lu, Yan A1 - Ma, Yu-qiang A1 - Chen, Guosong A1 - Jiang, Ming T1 - CO2-switchable response of protein microtubules BT - behaviour and mechanism JF - Materials chemistry frontiers N2 - Recently, we proposed a small molecular inducing ligand strategy to assemble proteins into highly-ordered structures via dual non-covalent interactions, i.e. carbohydrate-protein interaction and dimerization of Rhodamine B. Using this approach, artificial protein microtubules were successfully constructed. In this study, we find that these microtubules exhibit a perfect CO2 responsiveness; assembly and disassembly of these microtubules were nicely controlled by the alternative passage of CO2 and N-2. Upon the injection of CO2, a negative net-charged SBA turns into a neutral or positive net-charged SBA, which elongated, to some extent, the effective distance between SBA and Rhodamine B, resulting in the disassociation of the Rhodamine B dimer. Further experimental and simulation results reveal that the CO2-responsive mechanism differs from that of solubility change of the previously reported CO2-responsive synthetic materials. Y1 - 2018 U6 - https://doi.org/10.1039/c8qm00245b SN - 2052-1537 VL - 2 IS - 9 SP - 1642 EP - 1646 PB - Royal Society of Chemistry CY - Cambridge ER - TY - JOUR A1 - Yang, Guang A1 - Zheng, Wei A1 - Tao, Guoqing A1 - Wu, Libin A1 - Zhou, Qi-Feng A1 - Kochovski, Zdravko A1 - Ji, Tan A1 - Chen, Huaijun A1 - Li, Xiaopeng A1 - Lu, Yan A1 - Ding, Hong-ming A1 - Yang, Hai-Bo A1 - Chen, Guosong A1 - Jiang, Ming T1 - Diversiform and Transformable Glyco-Nanostructures Constructed from Amphiphilic Supramolecular Metallocarbohydrates through Hierarchical Self-Assembly: The Balance between Metallacycles and Saccharides JF - ACS nano N2 - During the past decade, self-assembly of saccharide-containing amphiphilic molecules toward bioinspired functional glycomaterials has attracted continuous attention due to their various applications in fundamental and practical areas. However, it still remains a great challenge to prepare hierarchical glycoassemblies with controllable and diversiform structures because of the complexity of saccharide structures and carbohydrate-carbohydrate interactions. Herein, through hierarchical self-assembly of modulated amphiphilic supramolecular metallocarbohydrates, we successfully prepared various well-defined glyco-nanostructures in aqueous solution, including vesicles, solid spheres, and opened vesicles depending on the molecular structures of metallocarbohydrates. More attractively, these glyco-nanostructures can further transform into other morphological structures in aqueous solutions such as worm-like micelles, tubules, and even tupanvirus-like vesicles (TVVs). It is worth mentioning that distinctive anisotropic structures including the opened vesicles (OVs) and TVVs were rarely reported in glycobased nano-objects. This intriguing diversity was mainly controlled by the subtle structural trade-off of the two major components of the amphiphiles, i.e., the saccharides and metallacycles. To further understand this precise structural control, molecular simulations provided deep physical insights on the morphology evolution and balancing of the contributions from saccharides and metallacycles. Moreover, the multivalency of glyco-nanostructures with different shapes and sizes was demonstrated by agglutination with a diversity of sugarbinding protein receptors such as the plant lectins Concanavalin A (ConA). This modular synthesis strategy provides access to systematic tuning of molecular structure and self-assembled architecture, which undoubtedly will broaden our horizons on the controllable fabrication of biomimetic glycomaterials such as biological membranes and supramolecular lectin inhibitors. KW - glycomaterials KW - diversiform structures KW - hierarchical self-assembly KW - metallocarbohydrates KW - anisotropic structures Y1 - 2019 U6 - https://doi.org/10.1021/acsnano.9b07134 SN - 1936-0851 SN - 1936-086X VL - 13 IS - 11 SP - 13474 EP - 13485 PB - American Chemical Society CY - Washington ER -