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Title: Kinetically Controlled Nanostructure Formation in Self-Assembled Globular Protein–Polymer Diblock Copolymers

Abstract

Aqueous processing of globular protein–polymer diblock copolymers into solid-state materials and subsequent solvent annealing enables kinetic and thermodynamic control of nanostructure formation to produce block copolymer morphologies that maintain a high degree of protein fold and function. When model diblock copolymers composed of mCherry-b-poly(N-isopropylacrylamide) are used, orthogonal control over solubility of the protein block through changes in pH and the polymer block through changes in temperature is demonstrated during casting and solvent annealing. Hexagonal cylinders, perforated lamellae, lamellae, or hexagonal and disordered micellar phases are observed, depending on the coil fraction of the block copolymer and the kinetic pathway used for self-assembly. Here, good solvents for the polymer block produce ordered structures reminiscent of coil–coil diblock copolymers, while an unfavorable solvent results in kinetically trapped micellar structures. Decreasing solvent quality for the protein improves long-range ordering, suggesting that the strength of protein interactions influences nanostructure formation. Subsequent solvent annealing results in evolution of the nanostructures, with the best ordering and the highest protein function observed when annealing in a good solvent for both blocks. While protein secondary structure was found to be almost entirely preserved for all processing pathways, UV–vis spectroscopy of solid-state films indicates that using a good solventmore » for the protein block enables up to 70% of the protein to be retained in its functional form.« less

Authors:
 [1];  [1];  [1]
  1. Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1069699
Report Number(s):
BNL-100271-2013-JA
Journal ID: ISSN 1525-7797
Grant/Contract Number:  
AC02-98CH10886
Resource Type:
Accepted Manuscript
Journal Name:
Biomacromolecules
Additional Journal Information:
Journal Volume: 13; Journal Issue: 9; Journal ID: ISSN 1525-7797
Publisher:
American Chemical Society
Country of Publication:
United States
Language:
English
Subject:
77 NANOSCIENCE AND NANOTECHNOLOGY; block copolymer; self-assembly; protein-polymer conjugate; mCherry; PNIPAM

Citation Formats

Thomas, Carla S., Xu, Liza, and Olsen, Bradley D. Kinetically Controlled Nanostructure Formation in Self-Assembled Globular Protein–Polymer Diblock Copolymers. United States: N. p., 2012. Web. doi:10.1021/bm300763x.
Thomas, Carla S., Xu, Liza, & Olsen, Bradley D. Kinetically Controlled Nanostructure Formation in Self-Assembled Globular Protein–Polymer Diblock Copolymers. United States. doi:10.1021/bm300763x.
Thomas, Carla S., Xu, Liza, and Olsen, Bradley D. Tue . "Kinetically Controlled Nanostructure Formation in Self-Assembled Globular Protein–Polymer Diblock Copolymers". United States. doi:10.1021/bm300763x. https://www.osti.gov/servlets/purl/1069699.
@article{osti_1069699,
title = {Kinetically Controlled Nanostructure Formation in Self-Assembled Globular Protein–Polymer Diblock Copolymers},
author = {Thomas, Carla S. and Xu, Liza and Olsen, Bradley D.},
abstractNote = {Aqueous processing of globular protein–polymer diblock copolymers into solid-state materials and subsequent solvent annealing enables kinetic and thermodynamic control of nanostructure formation to produce block copolymer morphologies that maintain a high degree of protein fold and function. When model diblock copolymers composed of mCherry-b-poly(N-isopropylacrylamide) are used, orthogonal control over solubility of the protein block through changes in pH and the polymer block through changes in temperature is demonstrated during casting and solvent annealing. Hexagonal cylinders, perforated lamellae, lamellae, or hexagonal and disordered micellar phases are observed, depending on the coil fraction of the block copolymer and the kinetic pathway used for self-assembly. Here, good solvents for the polymer block produce ordered structures reminiscent of coil–coil diblock copolymers, while an unfavorable solvent results in kinetically trapped micellar structures. Decreasing solvent quality for the protein improves long-range ordering, suggesting that the strength of protein interactions influences nanostructure formation. Subsequent solvent annealing results in evolution of the nanostructures, with the best ordering and the highest protein function observed when annealing in a good solvent for both blocks. While protein secondary structure was found to be almost entirely preserved for all processing pathways, UV–vis spectroscopy of solid-state films indicates that using a good solvent for the protein block enables up to 70% of the protein to be retained in its functional form.},
doi = {10.1021/bm300763x},
journal = {Biomacromolecules},
number = 9,
volume = 13,
place = {United States},
year = {2012},
month = {8}
}

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