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

Henrik K. Munch, Jesper Nygaard, Niels Johan Christensen, Christian Engelbrekt, Mads Østergaard, Trine Porsgaard, Thomas Hoeg-Jensen, Jingdong Zhang, Lise Arleth, Peter W. Thulstrup, Knud Jørgen Jensen

Research output: Contribution to journalJournal articleResearchpeer-review

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 ZnII-binding hexamers to SA into trimers of hexamers, [[HI–bipy]6]3, driven by octahedral coordination to a FeII 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 FeII than ZnII ions, enabling control of the hexamer formation with ZnII and the formation of trimers of hexamers with FeII ions. This precise control of protein SA to give oligomers of oligomers provides nanoscale structures with potential applications in nanomedicine.
Original languageEnglish
JournalAngewandte Chemie
Volume128
Issue number7
Pages (from-to)2424-2427
Number of pages4
ISSN0044-8249
DOIs
Publication statusPublished - 2016

Keywords

  • INSULIN
  • Kleinwinkel-Röntgenstreuung
  • Nanostrukturen
  • Rastersondenverfahren
  • Selbstorganisation

Cite this

Munch, H. K., Nygaard, J., Christensen, N. J., Engelbrekt, C., Østergaard, M., Porsgaard, T., ... Jensen, K. J. (2016). Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites. Angewandte Chemie, 128(7), 2424-2427. https://doi.org/10.1002/ange.201509088
Munch, Henrik K. ; Nygaard, Jesper ; Christensen, Niels Johan ; Engelbrekt, Christian ; Østergaard, Mads ; Porsgaard, Trine ; Hoeg-Jensen, Thomas ; Zhang, Jingdong ; Arleth, Lise ; Thulstrup, Peter W. ; Jensen, Knud Jørgen. / Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites. In: Angewandte Chemie. 2016 ; Vol. 128, No. 7. pp. 2424-2427.
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title = "Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites",
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 ZnII-binding hexamers to SA into trimers of hexamers, [[HI–bipy]6]3, driven by octahedral coordination to a FeII 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 FeII than ZnII ions, enabling control of the hexamer formation with ZnII and the formation of trimers of hexamers with FeII ions. This precise control of protein SA to give oligomers of oligomers provides nanoscale structures with potential applications in nanomedicine.",
keywords = "INSULIN, Kleinwinkel-R{\"o}ntgenstreuung, Nanostrukturen, Rastersondenverfahren, Selbstorganisation",
author = "Munch, {Henrik K.} and Jesper Nygaard and Christensen, {Niels Johan} and Christian Engelbrekt and Mads {\O}stergaard and Trine Porsgaard and Thomas Hoeg-Jensen and Jingdong Zhang and Lise Arleth and Thulstrup, {Peter W.} and Jensen, {Knud J{\o}rgen}",
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doi = "10.1002/ange.201509088",
language = "English",
volume = "128",
pages = "2424--2427",
journal = "Angewandte Chemie",
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Munch, HK, Nygaard, J, Christensen, NJ, Engelbrekt, C, Østergaard, M, Porsgaard, T, Hoeg-Jensen, T, Zhang, J, Arleth, L, Thulstrup, PW & Jensen, KJ 2016, 'Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites', Angewandte Chemie, vol. 128, no. 7, pp. 2424-2427. https://doi.org/10.1002/ange.201509088

Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites. / Munch, Henrik K.; Nygaard, Jesper; Christensen, Niels Johan; Engelbrekt, Christian; Østergaard, Mads; Porsgaard, Trine; Hoeg-Jensen, Thomas; Zhang, Jingdong; Arleth, Lise; Thulstrup, Peter W.; Jensen, Knud Jørgen.

In: Angewandte Chemie, Vol. 128, No. 7, 2016, p. 2424-2427.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites

AU - Munch, Henrik K.

AU - Nygaard, Jesper

AU - Christensen, Niels Johan

AU - Engelbrekt, Christian

AU - Østergaard, Mads

AU - Porsgaard, Trine

AU - Hoeg-Jensen, Thomas

AU - Zhang, Jingdong

AU - Arleth, Lise

AU - Thulstrup, Peter W.

AU - Jensen, Knud Jørgen

PY - 2016

Y1 - 2016

N2 - 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 ZnII-binding hexamers to SA into trimers of hexamers, [[HI–bipy]6]3, driven by octahedral coordination to a FeII 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 FeII than ZnII ions, enabling control of the hexamer formation with ZnII and the formation of trimers of hexamers with FeII ions. This precise control of protein SA to give oligomers of oligomers provides nanoscale structures with potential applications in nanomedicine.

AB - 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 ZnII-binding hexamers to SA into trimers of hexamers, [[HI–bipy]6]3, driven by octahedral coordination to a FeII 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 FeII than ZnII ions, enabling control of the hexamer formation with ZnII and the formation of trimers of hexamers with FeII ions. This precise control of protein SA to give oligomers of oligomers provides nanoscale structures with potential applications in nanomedicine.

KW - INSULIN

KW - Kleinwinkel-Röntgenstreuung

KW - Nanostrukturen

KW - Rastersondenverfahren

KW - Selbstorganisation

U2 - 10.1002/ange.201509088

DO - 10.1002/ange.201509088

M3 - Journal article

VL - 128

SP - 2424

EP - 2427

JO - Angewandte Chemie

JF - Angewandte Chemie

SN - 0044-8249

IS - 7

ER -