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

Malmström, Jenny; Wason, Akshita; Roache, Fergus J M; Yewdall, N. Amy; Radjainia, Mazdak; Wei, Shanghai; Higgins, Michael J.; Williams, David E.; Gerrard, Juliet A.; Travaš-Sejdić, Jadranka

doi:10.1039/c5nr05476a

Cited by 12 publications

(25 citation statements)

References 59 publications

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“…In addition, the diverse chemistry available through the polypeptide chain can be exploited to introduce non-native functionalities in these nanoconstructs. [5][6][7] The high degree of precision of protein assembly can also be used in a unique way to order other nanocomponents in multiple dimensions, 1,[8][9][10] such as nanoparticle organization for plasmonic devices. 11 In the ordering of nanoscale building blocks for nanodevices such as bioelectronics and biomaterials, protein-surface interactions are an important consideration.…”

Section: Introductionmentioning

confidence: 99%

Formation of supramolecular protein structures on gold surfaces

et al. 2017

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Recent research has highlighted the exciting possibilities enabled by the use of protein structures as nanocomponents to form functional nanodevices. To this end, control over protein-protein and protein-surface interactions is essential. In this study, the authors probe the interaction of human peroxiredoxin 3 with gold surfaces, a protein that has been previously identified as having potential use in nanotechnology. Analytical ultracentrifugation and transmission electron microscopy revealed the pH mediated assembly of protein toroids into tubular structures across a small pH range. Quartz crystal microbalance with dissipation measurements showed differences in absorbed protein mass when pH is switched from pH 8.0 to 7.2, in line with the formation of supramolecular structures observed in solution studies. Scanning tunneling microscopy under ambient conditions showed that these protein tubes form on surfaces in a concentration dependent manner, with a tendency for protein adsorption and supramolecular assembly at the edges of Au(111) terraces. Finally, self-assembled monolayer modification of Au surfaces was explored as a means to control the adsorption and orientation of pH triggered protein structures.

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Section: Introductionmentioning

confidence: 99%

Formation of supramolecular protein structures on gold surfaces

et al. 2017

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“…They focused on atomic force microscopy (AFM), , time-of-flight secondary ion mass spectrometry (ToF-SIMS), , neutron reflectometry (NR), and spectroscopic ellipsometry (SE) . In particular, AFM results to be one of the most promising characterization strategies since this it is very effective in studying nanosized objects, − including biomolecules, − with nanometer and subnanometer resolution. For instance, tapping mode AFM has been used to image immunoglobulins on mica surfaces, finding that it is possible resolving the three-domain structure of the antibody (Ab) and distinguishing between different protein morphologies and orientations.…”

Section: Introductionmentioning

confidence: 99%

Single Molecule Characterization of UV-Activated Antibodies on Gold by Atomic Force Microscopy

et al. 2016

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The interaction between proteins and solid surfaces can influence their conformation and therefore also their activity and affinity. These interactions are highly specific for the respective combination of proteins and solids. Consequently, it is desirable to investigate the conformation of proteins on technical surfaces, ideally at single molecule level, and to correlate the results with their activity. This is in particular true for biosensors where the conformation-dependent target affinity of an immobilized receptor determines the sensitivity of the sensor. Here, we investigate for the first time the immobilization and orientation of antibodies (Abs) photoactivated by a photonic immobilization technique (PIT), which has previously demonstrated to enhance binding capabilities of antibody receptors. The photoactivated immunoglobulins are immobilized on ultrasmooth template stripped gold films and investigated by atomic force microscopy (AFM) at the level of individual molecules. The observed protein orientations are compared with results of nonactivated antibodies adsorbed on similar gold films and mica reference samples. We find that the behavior of Abs is similar for mica and gold when the protein are not treated (physisorption), whereas smaller contact area and larger heights are measured when Abs are treated (PIT). This is explained by assuming that the activated antibodies tend to be more upright compared with nonirradiated ones, thereby providing a better exposure of the binding sites. This finding matches the observed enhancement of Abs binding efficiency when PIT is used to functionalize gold surface of QCM-based biosensors.

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“…Their approach allows for the fabrication of thin films combining the properties of both synthetic and biological building units. 31 Additionally, Malmstrom et al 32 showed that protein leaches out of the thin film upon exposure to water. This could be relevant for the release of active biomolecules in drug delivery applications.…”

Section: ■ Introductionmentioning

confidence: 99%

Polystyrene-block-poly(ethylene oxide) Thin Films Fabricated from a Solvent Mixture for the Co-Assembly of Polymers and Proteins

Kollmetz

Gerrard

et al. 2020

ACS Omega

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The co-assembly of peptides and proteins in poly(styrene- block -ethylene oxide) (PS- b -PEO) thin films has proven to be a promising method to fabricate polymer–biomolecule functional materials. Contrary to the covalent immobilization of biomolecules on surfaces, co-assembly presents the opportunity to arrange cargo within thin films, which can be released upon exposure to an aqueous environment. The use of a mixed solvent system ensures the solubilization of hydrophobic polymer as well as the solubilization and protection of the biomolecule cargo. However, to produce largely defect-free films of PS- b -PEO from a solvent mixture containing water is challenging due to the narrow range of solvent miscibility and polymer/protein solubility. This work explores the limits of using a benzene/methanol/water solvent mixture for the production of thin PS- b -PEO films and provides a template for the fabrication optimization of block copolymer thin films in different complex solvent systems. The film quality is analyzed using optical microscopy and atomic force microscopy and correlated to the solvent composition. By adjusting the solvent composition to 80/18.8/1.2 vol % benzene/methanol/water, it was possible to reliably fabricate thin films with less than 1% macroscopic defect surface coverage. Using the optimized solvent composition, we also demonstrate the fabrication of ordered PS- b -PEO films containing lysozyme. Furthermore, we show the release of lysozyme into aqueous media, which highlights the potential use of such films for drug delivery applications.

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

Cited by 12 publications

References 59 publications

Formation of supramolecular protein structures on gold surfaces

Formation of supramolecular protein structures on gold surfaces

Single Molecule Characterization of UV-Activated Antibodies on Gold by Atomic Force Microscopy

Polystyrene-block-poly(ethylene oxide) Thin Films Fabricated from a Solvent Mixture for the Co-Assembly of Polymers and Proteins

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