skip to main content
DOE PAGES title logo U.S. Department of Energy
Office of Scientific and Technical Information

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:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 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. https://doi.org/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. https://doi.org/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. https://doi.org/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}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record

Citation Metrics:
Cited by: 48 works
Citation information provided by
Web of Science

Save / Share:

Works referencing / citing this record:

Self-Assembly of Globular-Protein-Containing Block Copolymers
journal, July 2013


Topological Effects on Globular Protein-ELP Fusion Block Copolymer Self-Assembly
journal, December 2014

  • Qin, Guokui; Glassman, Matthew J.; Lam, Christopher N.
  • Advanced Functional Materials, Vol. 25, Issue 5
  • DOI: 10.1002/adfm.201403453

Self-Assembly of Globular-Protein-Containing Block Copolymers
journal, July 2013


Phase transitions in concentrated solution self-assembly of globular protein–polymer block copolymers
journal, January 2013

  • Lam, Christopher N.; Olsen, Bradley D.
  • Soft Matter, Vol. 9, Issue 8
  • DOI: 10.1039/c2sm27459k

Micellar‐Mediated Block Copolymer Ordering Dynamics Revealed by In Situ Grazing Incidence Small‐Angle X‐Ray Scattering during Spin Coating
journal, March 2019

  • Fleury, Guillaume; Hermida‐Merino, Daniel; Jingjin, Dong
  • Advanced Functional Materials, Vol. 29, Issue 10
  • DOI: 10.1002/adfm.201806741

Enzyme–Polymer Conjugates as Robust Pickering Interfacial Biocatalysts for Efficient Biotransformations and One‐Pot Cascade Reactions
journal, September 2018

  • Sun, Zhiyong; Glebe, Ulrich; Charan, Himanshu
  • Angewandte Chemie, Vol. 130, Issue 42
  • DOI: 10.1002/ange.201806049

Enzyme–Polymer Conjugates as Robust Pickering Interfacial Biocatalysts for Efficient Biotransformations and One‐Pot Cascade Reactions
journal, October 2018

  • Sun, Zhiyong; Glebe, Ulrich; Charan, Himanshu
  • Angewandte Chemie International Edition, Vol. 57, Issue 42
  • DOI: 10.1002/anie.201806049

Block copolymers for protein ordering
journal, January 2014

  • Malmström, Jenny; Travas-Sejdic, Jadranka
  • Journal of Applied Polymer Science, Vol. 131, Issue 14
  • DOI: 10.1002/app.40360

Photochemistry for Well-Defined Polymers in Aqueous Media: From Fundamentals to Polymer Nanoparticles to Bioconjugates
journal, May 2018

  • Burridge, Kevin M.; Wright, Thaiesha A.; Page, Richard C.
  • Macromolecular Rapid Communications, Vol. 39, Issue 12
  • DOI: 10.1002/marc.201800093

Self-assembled nanostructures from amphiphilic globular protein–polymer hybrids
journal, September 2017


Responsive polymers for biosensing and protein delivery
journal, January 2014

  • Islam, Molla R.; Gao, Yongfeng; Li, Xue
  • J. Mater. Chem. B, Vol. 2, Issue 17
  • DOI: 10.1039/c3tb21657h

Elastin-like polypeptides as building motifs toward designing functional nanobiomaterials
journal, January 2019

  • Le, Duc H. T.; Sugawara-Narutaki, Ayae
  • Molecular Systems Design & Engineering, Vol. 4, Issue 3
  • DOI: 10.1039/c9me00002j