@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}
}