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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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Jensen, Knud
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (4/4 displayed)
- 2016Construction of insulin 18-mer nanoassemblies driven by coordination to Iron(II) and Zinc(II) ions at distinct sitescitations
- 2016Dimeric peptides with three different linkers self-assemble with phospholipids to form peptide nanodiscs that stabilize membrane proteinscitations
- 2015Expression, receptor binding, and biophysical characterization of guinea pig insulin desB30citations
- 2013Self-assembly of designed coiled coil peptides studied by small-angle X-ray scattering and analytical ultracentrifugationcitations
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article
Construction of insulin 18-mer nanoassemblies driven by coordination to Iron(II) and Zinc(II) ions at distinct sites
Abstract
<p>Controlled self-assembly (SA) of proteins offers the possibility to tune their properties or to create new materials. Herein, we present the synthesis of a modified human insulin (HI) with two distinct metal-ion binding sites, one native, the other abiotic, enabling hierarchical SA through coordination with two different metal ions. Selective attachment of an abiotic 2,2′-bipyridine (bipy) ligand to HI, yielding HI-bipy, enabled Zn<sup>II</sup>-binding hexamers to SA into trimers of hexamers, [[HI-bipy]<sub>6</sub>]<sub>3</sub>, driven by octahedral coordination to a Fe<sup>II</sup> ion. The structures were studied in solution by small-angle X-ray scattering and on surfaces with AFM. The abiotic metal ligand had a higher affinity for Fe<sup>II</sup> than Zn<sup>II</sup> ions, enabling control of the hexamer formation with Zn<sup>II</sup> and the formation of trimers of hexamers with Fe<sup>II</sup> ions. This precise control of protein SA to give oligomers of oligomers provides nanoscale structures with potential applications in nanomedicine.</p>