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Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites.

Munch, Henrik K; Nygaard, Jesper LU ; Christensen, Niels Johan; Engelbrekt, Christian; Østergaard, Mads; Porsgaard, Trine; Hoeg-Jensen, Thomas; Zhang, Jingdong; Arleth, Lise and Thulstrup, Peter W, et al. (2016) In Angewandte Chemie (International edition) 55(7). p.2378-2381
Abstract
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(II) -binding hexamers to SA into trimers of hexamers, [[HI-bipy]6 ]3 , driven by octahedral coordination to a Fe(II) 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(II) than Zn(II) ions, enabling control... (More)
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(II) -binding hexamers to SA into trimers of hexamers, [[HI-bipy]6 ]3 , driven by octahedral coordination to a Fe(II) 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(II) than Zn(II) ions, enabling control of the hexamer formation with Zn(II) and the formation of trimers of hexamers with Fe(II) ions. This precise control of protein SA to give oligomers of oligomers provides nanoscale structures with potential applications in nanomedicine. (Less)
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publication status
published
subject
in
Angewandte Chemie (International edition)
volume
55
issue
7
pages
2378 - 2381
publisher
John Wiley & Sons
external identifiers
  • pmid:26762534
  • scopus:84954341798
  • wos:000369970500011
ISSN
1521-3773
DOI
10.1002/anie.201509088
language
English
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yes
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bc08e781-ed26-419a-b065-4f477e10ef59 (old id 8592181)
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2016-02-11 21:58:24
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2017-01-01 06:12:52
@article{bc08e781-ed26-419a-b065-4f477e10ef59,
  abstract     = {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(II) -binding hexamers to SA into trimers of hexamers, [[HI-bipy]6 ]3 , driven by octahedral coordination to a Fe(II) 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(II) than Zn(II) ions, enabling control of the hexamer formation with Zn(II) and the formation of trimers of hexamers with Fe(II) ions. This precise control of protein SA to give oligomers of oligomers provides nanoscale structures with potential applications in nanomedicine.},
  author       = {Munch, Henrik K and Nygaard, Jesper and Christensen, Niels Johan and Engelbrekt, Christian and Østergaard, Mads and Porsgaard, Trine and Hoeg-Jensen, Thomas and Zhang, Jingdong and Arleth, Lise and Thulstrup, Peter W and Jensen, Knud J},
  issn         = {1521-3773},
  language     = {eng},
  number       = {7},
  pages        = {2378--2381},
  publisher    = {John Wiley & Sons},
  series       = {Angewandte Chemie (International edition)},
  title        = {Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites.},
  url          = {http://dx.doi.org/10.1002/anie.201509088},
  volume       = {55},
  year         = {2016},
}