TY  - JOUR
A1  - Qi, Wenjing
A1  - Zhang, Yufei
A1  - Kochovski, Zdravko
A1  - Wang, Jue
A1  - Lu, Yan
A1  - Chen, Guosong
A1  - Jiang, Ming
T1  - Self-assembly of Human Galectin-1 via dual supramolecular interactions and its inhibition of T-cell agglutination and apoptosis
JF  - Nano Research
N2  - 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.
KW  - protein self-assembly
KW  - supramolecular interactions
KW  - galectin
KW  - cell agglutination
Y1  - 2018
U6  - https://doi.org/10.1007/s12274-018-2169-7
SN  - 1998-0124
SN  - 1998-0000
VL  - 11
IS  - 10
SP  - 5566
EP  - 5572
PB  - Tsinghua Univ Press
CY  - Beijing
ER  -