Abstract Proteins self-assemble into kinds of sophisticated architectures is ubiquitous in nature. Construction of these nanostructures in laboratory is helpful for understanding this physiological process and obtaining new functional materials.… Click to show full abstract
Abstract Proteins self-assemble into kinds of sophisticated architectures is ubiquitous in nature. Construction of these nanostructures in laboratory is helpful for understanding this physiological process and obtaining new functional materials. Although current state-of-the-art strategies have been developed, effective methods to regulate the process are still deficient. Herein, hierarchical self-assembly of Con A induced by a new designed oligosaccharide inducing ligand (RhB-triMan) was reported. The self-assembly of Con A can be regulated in the presence of transition metal ion Mn2+ due to the opening of spirolactone of RhB, and the assembly process can be further regulated by changing the molar ratio of ligands to proteins.
               
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