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Path-Dependent Anisotropic Colloidal Assembly of Magnetic Nanocomposite-Protein Complexes.
Yanbai Pei1, Shengming Wu1, Peng Wang1
1The Institute for Translational Nanomedicine, Shanghai East Hospital, the Institute for Biomedical Engineering and Nano Science, School of Medicine, Tongji University, Shanghai 200092, P. R. China.
Langmuir : the ACS Journal of Surfaces and Colloids
|May 13, 2022
Summary
We demonstrate a novel method for creating micron-sized anisotropic magnetic nanoparticle assemblies using protein interactions. This controllable self-assembly process, triggered by protein concentration, offers a recyclable pathway for advanced nanomaterials.
Area of Science:
- Materials Science
- Nanotechnology
- Biomaterials Engineering
Background:
- Anisotropic self-assembly of nanoparticles (NPs) is crucial for advanced material design, driven by surface functionality and inter-particle interactions.
- Existing strategies utilize ligand interactions, protein interactions, or external stimuli, but controlled assembly of magnetic NPs into micron-sized anisotropic structures via protein interactions remains challenging.
Purpose of the Study:
- To elucidate the path-dependent self-assembly of magnetic iron oxide-silica (Fe3O4@SiO2) nanocomposites induced by NP-protein and protein-protein interactions.
- To investigate the role of protein concentration and type in forming micron-sized anisotropic colloidal assemblies.
Main Methods:
- Utilized 100 nm Fe3O4@SiO2 nanocomposites undergoing serial, independent induction of NP-protein interaction, magnetic force, and protein corona intermolecular interaction.
- Investigated the influence of protein concentration and specific serum proteins (fibrinogen, bovine serum albumin) on assembly dynamics.
- Explored the dissociation and recycling of the assembled structures using electrolytes.
Main Results:
- Achieved reproducible, controllable formation of dynamic, micron-sized anisotropic magnetic assemblies in a continuous medium.
- Identified NP-protein complex formation (aided by ions) as a prerequisite, followed by magnetic pre-organization and protein-mediated elongation.
- Demonstrated that protein concentration is more critical than protein structure for assembly; assemblies can be rapidly dissociated and recycled.
Conclusions:
- Developed a robust method for anisotropic colloidal assembly of magnetic NPs driven by a combination of magnetic forces and protein intermolecular interactions.
- The study highlights the pivotal role of protein concentration in controlling NP self-assembly and offers a recyclable system for magnetic nanomaterials.
