Self-assembly of Human Galectin-1 via dual supramolecular interactions and its inhibition of T-cell agglutination and apoptosis
- 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-cellRecently, 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.…
Verfasserangaben: | Wenjing QiGND, Yufei Zhang, Zdravko KochovskiORCiD, Jue Wang, Yan LuORCiDGND, Guosong Chen, Ming Jiang |
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DOI: | https://doi.org/10.1007/s12274-018-2169-7 |
ISSN: | 1998-0124 |
ISSN: | 1998-0000 |
Titel des übergeordneten Werks (Englisch): | Nano Research |
Verlag: | Tsinghua Univ Press |
Verlagsort: | Beijing |
Publikationstyp: | Wissenschaftlicher Artikel |
Sprache: | Englisch |
Datum der Erstveröffentlichung: | 28.08.2018 |
Erscheinungsjahr: | 2018 |
Datum der Freischaltung: | 17.09.2021 |
Freies Schlagwort / Tag: | cell agglutination; galectin; protein self-assembly; supramolecular interactions |
Band: | 11 |
Ausgabe: | 10 |
Seitenanzahl: | 7 |
Erste Seite: | 5566 |
Letzte Seite: | 5572 |
Fördernde Institution: | National Natural Science Foundation of ChinaNational Natural Science Foundation of China [51721002, 21504016, 91527305] |
Organisationseinheiten: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie |
DDC-Klassifikation: | 5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften |
Peer Review: | Referiert |