Directed co-assembly of hemeproteins with amphiphilic block copolymers toward functional biomolecular materials

Presley, Andrew D.; Chang, Jaerak; Xu, Ting

doi:10.1039/c0sm00817f

Cited by 37 publications

(53 citation statements)

References 55 publications

(68 reference statements)

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“…We have established protocols and explored characterization methods for these protein/polymer composite samples utilizing a unique stackable protein ring. The work here builds on previous studies using model protein such as ferritin 9 (which was nicely demonstrated to reside in the PEO domains) and myoglobin 11 (which has a strong UV-spectrum and enzymatic activity to employ for characterization). Future fine tuning of the assembly of the higher order Lsmα stacks within the PEO nanocontainers, along with the prospect of functionalizing the protein structures with for example noble metal particles opens up the possibility of exciting applications as functional electronic or optical materials.…”

Section: Resultsmentioning

confidence: 99%

“…The PEGylated protein was subsequently dialysed to water and freeze-dried before co-dissolving with the block copolymer. In order to protect the protein from denaturation, we followed the work by Presley et al, 11 who demonstrated the success of a mixed solvent system incorporating water, methanol and benzene. Using a similar protocol, a small amount of methanol/water mix was first added to the dry protein, followed by more methanol and finally the PS-b-PEO (1% in benzene), resulting in a completely clear solution (solvent composition 71.7% benzene, 26.9% methanol and 1.4% water, denoted control solvent).…”

Section: Resultsmentioning

confidence: 99%

“…Poly(styrene-blockethylene oxide) (PS-b-PEO, M n × 10 3 18.0-b-7.5) is used in this study and forms solvent-induced ordered films of hexagonally packed vertical cylinders of PEO, into which we aim to assemble the protein (Scheme 1). This polymer has not only been shown to be very robust in forming the desired phase, 42 but has also been used previously for co-assembly with both peptides 11 and protein-polymer conjugates such as ferritin 9 and myoglobin. 11 For the protein used in this study unambiguous characterisation of these structures is difficult; however in this work we provide extensive AFM and TEM imaging which confirm the successful incorporation of the protein into the PEO blocks and thus constitute a highly ordered and functionalisable matrix with potential downstream applications in advanced materials.…”

Section: Introductionmentioning

confidence: 99%

“…Ordered block copolymer films have been used for pattern transfer through etching or evaporation 5 and have also been explored as a template for directed nanoparticle assembly 6 and for biomolecule patterning on top of 7,8 or within. 6,7,[9][10][11][12][13][14] Peptides or proteins have also been used as one block of block copolymers and shown to self-assemble into ordered structures. [15][16][17][18][19] Biomolecules are generally believed to be good candidates for nanotechnology due to their versatility, small size and precise control over self-assembly.…”

Section: Introductionmentioning

confidence: 99%

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Protein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin films

et al. 2015

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This study explores the use of block copolymer self-assembly to organize Lsmα, a protein which forms stable doughnut-shaped heptameric structures. Here, we have explored the idea that 2-D crystalline arrays of protein filaments can be prepared by stacking doughnut shaped Lsmα protein into the poly(ethylene oxide) blocks of a hexagonal microphase-separated polystyrene-b-polyethylene oxide (PS-b-PEO) block copolymer. We were able to demonstrate the coordinated assembly of such a complex hierarchical nanostructure. The key to success was the choice of solvent systems and protein functionalization that achieved sufficient compatibility whilst still promoting assembly. Unambiguous characterisation of these structures is difficult; however AFM and TEM measurements confirmed that the protein was sequestered into the PEO blocks. The use of a protein that assembles into stackable doughnuts offers the possibility of assembling nanoscale optical, magnetic and electronic structures. This study explores the use of block copolymer self-assembly to organize Lsmα, a protein which forms stable doughnut-shaped heptameric structures. Here, we have explored the idea that 2-D crystalline arrays of protein filaments can be prepared by stacking doughnut shaped Lsmα protein into the poly(ethylene oxide) blocks of a hexagonal microphase-separated polystyrene-b-polyethylene oxide (PSb-PEO) block copolymer. We were able to demonstrate the coordinated assembly of such a complex hierarchical nanostructure. The key to success was the choice of solvent systems and protein functionalization that achieved sufficient compatibility whilst still promoting assembly. Unambiguous characterisation of these structures is difficult; however AFM and TEM measurements confirmed that the protein was sequestered into the PEO blocks. The use of a protein that assembles into stackable doughnuts offers the possibility of assembling nanoscale optical, magnetic and electronic structures.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Protein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin films

et al. 2015

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“…In a third approach, nanostructured templates are self-assembled from amphiphilic molecules and the proteins are inserted into the templates. This type of template has been demonstrated with the use of block copolymer thin films, 30 nanostructures formed from surfactants in solution, 31 and through the self-assembly of lipid materials. 32 …”

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confidence: 99%

Solid-State Nanostructured Materials from Self-Assembly of a Globular Protein–Polymer Diblock Copolymer

2011

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Self-assembly of three-dimensional solid-state nanostructures containing approximately 33% by weight globular protein is demonstrated using a globular protein-polymer diblock copolymer, providing a route to direct nanopatterning of proteins for use in bioelectronic and biocatalytic materials. A mutant red fluorescent protein, mCherryS131C, was prepared by incorporation of a unique cysteine residue and site-specifically conjugated to end-functionalized poly(N-isopropylacrylamide) through thiol-maleimide coupling to form a well-defined model protein-polymer block copolymer. The block copolymer was self-assembled into bulk nanostructures by solvent evaporation from concentrated solutions. Small-angle X-ray scattering and transmission electron microscopy illustrated the formation of highly disordered lamellae or hexagonally perforated lamellae depending upon the selectivity of the solvent during evaporation. Solvent annealing of bulk samples resulted in a transition towards lamellar nanostructures with mCherry packed in a bilayer configuration and a large improvement in long range ordering. Wide-angle X-ray scattering indicated that mCherry did not crystallize within the block copolymer nanodomains and that the β-sheet spacing was not affected by self-assembly. Circular dichroism showed no change in protein secondary structure after self-assembly, while UV-vis spectroscopy indicated approximately 35% of the chromophore remained optically active.

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Topological Effects on Globular Protein‐ELP Fusion Block Copolymer Self‐Assembly

Qin

Glassman

Lam

et al. 2014

Adv Funct Materials

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Perfectly defi ned, monodisperse fusion protein block copolymers of a thermoresponsive coil-like protein, ELP, and a globular protein, mCherry, are demonstrated to act as fully biosynthetic analogues to protein-polymer conjugates that can self-assemble into biofunctional nanostructures such as hexagonal and lamellar phases in concentrated solutions. The phase behavior of two mCherry-ELP fusions, E 10 -mCherry-E 10 and E 20 -mCherry, is investigated to compare linear and bola fusion self-assembly both in diluted and concentrated aqueous solution. In dilute solution, the molecular topology impacts the stability of micelles formed above the thermal transition temperature of the ELP block, with the diblock forming micelles and the bola forming unstable aggregates. Despite the chemical similarity of the two protein blocks, the materials order into block copolymer-like nanostructures across a wide range of concentrations at 30 wt% and above, with the bola fusion having a lower order-disorder transition concentration than the diblock fusion. The topology of the molecule has a large impact on the type of nanostructure formed, with the two fusions forming phases in the opposite order as a function of temperature and concentration. This new system provides a rich landscape to explore the capabilities of fusion architecture to control supramolecular assemblies for bioactive materials.

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Directed co-assembly of hemeproteins with amphiphilic block copolymers toward functional biomolecular materials

Cited by 37 publications

References 55 publications

Protein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin films

Protein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin films

Solid-State Nanostructured Materials from Self-Assembly of a Globular Protein–Polymer Diblock Copolymer

Topological Effects on Globular Protein‐ELP Fusion Block Copolymer Self‐Assembly

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