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| Azevedo, Nuno Monteiro |
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Porsgaard, Trine
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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>