Article Title

Self-assembly of Human Galectin-1 via dual supramolecular interactions and its inhibition of T-cell agglutination and apoptosis

Authors

Wenjing Qi, The State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200438, China
Yufei Zhang, The State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200438, China
Zdravko Kochovski, Soft Matter and Functional Materials, Helmholtz-Zentrum Berlin für Materialien und Energie, Berlin 14109, Germany
Jue Wang, The State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200438, China
Yan Lu, Soft Matter and Functional Materials, Helmholtz-Zentrum Berlin für Materialien und Energie, Berlin 14109, Germany Institute of Chemistry, University of Potsdam, 14476 Potsdam, Germany
Guosong Chen, The State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200438, China
Ming Jiang, The State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200438, China

Keywords

protein self-assembly, supramolecular interactions, galectin, cell agglutination

Abstract

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-tuned 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.

Graphical Abstract

DOI

https://doi.org/10.1007/s12274-018-2169-7

Publisher

Tsinghua University Press

Recommended Citation

Wenjing Qi,Yufei Zhang,Zdravko Kochovski,Jue Wang,Yan Lu,Guosong Chen,Ming Jiang, Self-assembly of Human Galectin-1 via dual supramolecular interactions and its inhibition of T-cell agglutination and apoptosis. NanoRes.2018, 11(10): 5566–5572