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Synthesis of Monodisperse Cylindrical Nanoparticles via Crystallization-driven Self-assembly of Biodegradable Block Copolymers
Published on: June 20, 2019
Kinetically controlled nanostructure formation in self-assembled globular protein-polymer diblock copolymers
Carla S Thomas1, Liza Xu, Bradley D Olsen
1Department of Chemical Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Biomacromolecules
|August 29, 2012
Summary
Researchers controlled protein-polymer nanostructure formation using aqueous processing and solvent annealing. This method preserves protein fold and function, yielding diverse morphologies like cylinders and lamellae.
Area of Science:
- Materials Science
- Biochemistry
- Polymer Chemistry
Background:
- Globular protein-polymer diblock copolymers offer unique properties for advanced materials.
- Controlling nanostructure formation is crucial for maintaining protein function in solid-state materials.
Purpose of the Study:
- To investigate aqueous processing and solvent annealing for controlling protein-polymer diblock copolymer nanostructures.
- To assess the impact of processing on protein fold and function within these materials.
Main Methods:
- Aqueous processing and solvent annealing of mCherry-b-poly(N-isopropylacrylamide) diblock copolymers.
- Orthogonal control of protein (pH) and polymer (temperature) solubility during self-assembly.
- Characterization of nanostructures and protein function using techniques like UV-vis spectroscopy.
Main Results:
- Diverse nanostructures (hexagonal cylinders, lamellae, micelles) were formed based on coil fraction and kinetic pathway.
- Good solvents for the polymer block yielded ordered structures, while unfavorable solvents led to kinetically trapped micelles.
- Solvent annealing in good solvents for both blocks maximized ordering and protein function (up to 70% retention).
Conclusions:
- Aqueous processing and solvent annealing provide kinetic and thermodynamic control over protein-polymer nanostructure formation.
- Protein secondary structure is largely preserved, and functional retention is significant when processing conditions are optimized.
- The strength of protein interactions and solvent quality critically influence nanostructure ordering and protein functionality.
