@article{YangDingKochovskietal.2017,
  author    = {Yang, Guang and Ding, Hong-ming and Kochovski, Zdravko and Hu, Rongting and Lu, Yan and Ma, Yu-qiang and Chen, Guosong and Jiang, Ming},
  title     = {Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {56},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.201703052},
  pages     = {10691 -- 10695},
  year      = {2017},
  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.},
  language  = {en}
}
@article{YangZhengTaoetal.2019,
  author    = {Yang, Guang and Zheng, Wei and Tao, Guoqing and Wu, Libin and Zhou, Qi-Feng and Kochovski, Zdravko and Ji, Tan and Chen, Huaijun and Li, Xiaopeng and Lu, Yan and Ding, Hong-ming and Yang, Hai-Bo and Chen, Guosong and Jiang, Ming},
  title     = {Diversiform and Transformable Glyco-Nanostructures Constructed from Amphiphilic Supramolecular Metallocarbohydrates through Hierarchical Self-Assembly: The Balance between Metallacycles and Saccharides},
  series = {ACS nano},
  volume    = {13},
  journal   = {ACS nano},
  number    = {11},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1936-0851},
  doi       = {10.1021/acsnano.9b07134},
  pages     = {13474 -- 13485},
  year      = {2019},
  abstract  = {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.},
  language  = {en}
}
@article{YangHuDingetal.2018,
  author    = {Yang, Guang and Hu, Rongting and Ding, Hong-ming and Kochovski, Zdravko and Mei, Shilin and Lu, Yan and Ma, Yu-qiang and Chen, Guosong and Jiang, Ming},
  title     = {CO2-switchable response of protein microtubules},
  series = {Materials chemistry frontiers},
  volume    = {2},
  journal   = {Materials chemistry frontiers},
  number    = {9},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2052-1537},
  doi       = {10.1039/c8qm00245b},
  pages     = {1642 -- 1646},
  year      = {2018},
  abstract  = {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.},
  language  = {en}
}
@article{QiZhangKochovskietal.2018,
  author    = {Qi, Wenjing and Zhang, Yufei and Kochovski, Zdravko and Wang, Jue and Lu, Yan and Chen, Guosong and Jiang, Ming},
  title     = {Self-assembly of Human Galectin-1 via dual supramolecular interactions and its inhibition of T-cell agglutination and apoptosis},
  series = {Nano Research},
  volume    = {11},
  journal   = {Nano Research},
  number    = {10},
  publisher = {Tsinghua Univ Press},
  address   = {Beijing},
  issn      = {1998-0124},
  doi       = {10.1007/s12274-018-2169-7},
  pages     = {5566 -- 5572},
  year      = {2018},
  abstract  = {Recently, we proposed a new strategy to construct artificial plant protein assemblies, which were induced by adding a small molecule, based on dual supramolecular interactions. In this paper, we further explored this method by employing Human Galectin-1 (Gal-1) as a building block to form self-assembled microribbons. Two non-covalent interactions, including lactose-lectin binding and dimerization of Rhodamine B (RhB), induced by the small molecule ligand addition, were involved in the crosslinking of the animal protein, resulting in the formation of assemblies. By using transmission electron microscopy (TEM), cryo-electron microscopy (cryo-EM), and three-dimensional (3D) tomographic analysis, we arrived at a possible mechanistic model for the microribbon formation. Furthermore, the morphology of protein assemblies could be fine-timed by varying the incubation time, the protein/ligand ratio, and the chemical structures of ligands. Interestingly, the formation of protein microribbons successfully inhibited Gal-1 induced T-cell agglutination and apoptosis. This is because the multivalent and dynamic interactions in protein assemblies compete with the binding between Gal-1 and the glycans on cell surfaces, which suppresses the function of Gal-1 in promotion of tumor progression and metastasis.},
  language  = {en}
}
@article{DuanZhouJiangetal.2021,
  author    = {Duan, Hongbo and Zhou, Sheng and Jiang, Kejun and Bertram, Christoph and Harmsen, Mathijs and Kriegler, Elmar and van Vuuren, Detlef P. and Wang, Shouyang and Fujimori, Shinichiro and Tavoni, Massimo and Ming, Xi and Keramidas, Kimon and Iyer, Gokul and Edmonds, James},
  title     = {Assessing China's efforts to pursue the 1.5°C warming limit},
  series = {Science},
  volume    = {372},
  journal   = {Science},
  number    = {6540},
  publisher = {American Association for the Advancement of Science},
  address   = {Washington, DC},
  issn      = {1095-9203},
  doi       = {10.1126/science.aba8767},
  pages     = {378 -- 385},
  year      = {2021},
  abstract  = {Given the increasing interest in keeping global warming below 1.5°C, a key question is what this would mean for China's emission pathway, energy restructuring, and decarbonization. By conducting a multimodel study, we find that the 1.5°C-consistent goal would require China to reduce its carbon emissions and energy consumption by more than 90 and 39\%, respectively, compared with the "no policy" case. Negative emission technologies play an important role in achieving near-zero emissions, with captured carbon accounting on average for 20\% of the total reductions in 2050. Our multimodel comparisons reveal large differences in necessary emission reductions across sectors, whereas what is consistent is that the power sector is required to achieve full decarbonization by 2050. The cross-model averages indicate that China's accumulated policy costs may amount to 2.8 to 5.7\% of its gross domestic product by 2050, given the 1.5°C warming limit.},
  language  = {en}
}