Construction of insulin 18-mer nanoassemblies driven by coordination to Iron(II) and Zinc(II) ions at distinct sites

Henrik Kofoed Munch; Jesper Nygård; Niels Johan Christensen; Christian Engelbrekt; Mads Østergaard; Trine Porsgaard; Thomas Hoeg-Jensen; Jingdong Zhang; Lise Arleth; Peter Waaben Thulstrup; Knud Jørgen Jensen

doi:10.1002/anie.201509088

Construction of insulin 18-mer nanoassemblies driven by coordination to Iron(II) and Zinc(II) ions at distinct sites

Henrik Kofoed Munch, Jesper Nygård, Niels Johan Christensen, Christian Engelbrekt, Mads Østergaard, Trine Porsgaard, Thomas Hoeg-Jensen, Jingdong Zhang, Lise Arleth, Peter Waaben Thulstrup, Knud Jørgen Jensen^*

^*Corresponding author for this work

7 Citations (Scopus)

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.

Original language	English
Journal	Angewandte Chemie International Edition
Volume	55
Issue number	7
Pages (from-to)	2378-2381
Number of pages	4
ISSN	1433-7851
DOIs	https://doi.org/10.1002/anie.201509088
Publication status	Published - 12 Feb 2016

Keywords

Atomic force microscopy
Insulin
Nanostructures
Self-assembly
Small-angle X-ray scattering

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https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/anie.201509088

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Munch, H. K., Nygård, J., Christensen, N. J., Engelbrekt, C., Østergaard, M., Porsgaard, T., Hoeg-Jensen, T., Zhang, J., Arleth, L., Thulstrup, P. W., & 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 International Edition, 55(7), 2378-2381. https://doi.org/10.1002/anie.201509088

Munch, HK, Nygård, 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 International Edition, vol. 55, no. 7, pp. 2378-2381. https://doi.org/10.1002/anie.201509088

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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 = "Atomic force microscopy, Insulin, Nanostructures, Self-assembly, Small-angle X-ray scattering",

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AU - Munch, Henrik Kofoed

AU - Nygård, 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 Waaben

AU - Jensen, Knud Jørgen

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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 - Atomic force microscopy

KW - Insulin

KW - Nanostructures

KW - Self-assembly

KW - Small-angle X-ray scattering

U2 - 10.1002/anie.201509088

DO - 10.1002/anie.201509088

M3 - Letter

C2 - 26762534

AN - SCOPUS:84954341798

SN - 1433-7851

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JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

IS - 7

ER -

Construction of insulin 18-mer nanoassemblies driven by coordination to Iron(II) and Zinc(II) ions at distinct sites

Abstract

Keywords

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