| People | Locations | Statistics |
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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Voets, Ilja
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (9/9 displayed)
- 2024Freezing-mediated formation of supraproteins using depletion forcescitations
- 2022Switchable Electrostatically Templated Polymerizationcitations
- 2021Single Enzyme Nanoparticles with Improved Biocatalytic Activity through Protein Entrapment in a Surfactant Shellcitations
- 2020Bioinspired Scaffolding by Supramolecular Amines Allows the Formation of One- and Two-Dimensional Silica Superstructurescitations
- 2018Supramolecular block copolymers under thermodynamic controlcitations
- 2015The coil-to-globule transition of single-chain polymeric nanoparticles with a chiral internal secondary structurecitations
- 2014Folding polymers with pendant hydrogen bonding motifs in water : the effect of polymer length and concentration on the shape and size of single-chain polymeric nanoparticlescitations
- 2013Sticky Supramolecular Grafts Stretch Single Polymer Chainscitations
- 2008Synthesis of novel well-defined poly(vinyl acetate)-b-poly(acrylonitrile) and derivatized water-soluble poly(vinyl alcohol)-b-poly(acrylic acid) block copolymers by cobalt-mediated radical polymerizationcitations
Places of action
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article
Single Enzyme Nanoparticles with Improved Biocatalytic Activity through Protein Entrapment in a Surfactant Shell
Abstract
<p>A polymeric corona consisting of an alkyl-glycolic acid ethoxylate (CXEOY) surfactant offers a promising approach toward endowing proteins with thermotropic phase behavior and hyperthermal activity. Typically, preparation of protein-surfactant biohybrids is performed via chemical modification of acidic residues followed by electrostatic conjugation of an anionic surfactant to encapsulate single proteins. While this procedure has been applied to a broad range of proteins, modification of acidic residues may be detrimental to function for specific enzymes. Herein, we report on the one-pot preparation of biohybrids via covalent conjugation of surfactants to accessible lysine residues. We entrap the model enzyme hen egg-white lysozyme (HEWL) in a shell of carboxyl-functionalized C12EO10 or C12EO22 surfactants. With fewer surfactants, our covalent biohybrids display similar thermotropic phase behavior to their electrostatically conjugated analogues. Through a combination of small-angle X-ray scattering and circular dichroism spectroscopy, we find that both classes of biohybrids consist of a folded single-protein core decorated by surfactants. Whilst traditional biohybrids retain densely packed surfactant coronas, our biohybrids display a less dense and heterogeneously distributed surfactant coverage located opposite to the catalytic cleft of HEWL. In solution, this surfactant coating permits 7- or 3.5-fold improvements in activity retention for biohybrids containing C12EO10 or C12EO22, respectively. The reported alternative pathway for biohybrid preparation offers a new horizon to expand upon the library of proteins for which functional biohybrid materials can be prepared. We also expect that an improved understanding of the distribution of tethered surfactants in the corona will be crucial for future structure-function investigations.</p>