Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites. Munch, H. K., Nygaard, J., Christensen, N. J., Engelbrekt, C., Ostergaard, M., Porsgaard, T., Hoeg-Jensen, T., Zhang, J., Arleth, L., Thulstrup, P. W., & Jensen, K. J. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 55(7):2378-2381, FEB 12, 2016.
doi  abstract   bibtex   
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 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.
@article{ISI:000369970500011,
	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 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.}},
	Author = {Munch, Henrik K. and Nygaard, Jesper and Christensen, Niels Johan and Engelbrekt, Christian and Ostergaard, Mads and Porsgaard, Trine and Hoeg-Jensen, Thomas and Zhang, Jingdong and Arleth, Lise and Thulstrup, Peter W. and Jensen, Knud J.},
	Date-Added = {2017-10-03 14:11:19 +0000},
	Date-Modified = {2017-10-03 14:11:19 +0000},
	Doi = {{10.1002/anie.201509088}},
	Eissn = {{1521-3773}},
	Issn = {{1433-7851}},
	Journal = {{ANGEWANDTE CHEMIE-INTERNATIONAL EDITION}},
	Month = {{FEB 12}},
	Number = {{7}},
	Orcid-Numbers = {{Jensen, Knud/0000-0003-3525-5452 Thulstrup, Peter/0000-0002-9241-4352 Christensen, Niels Johan/0000-0001-9588-2656 Zhang, Jingdong/0000-0002-0889-7057 Arleth, Lise/0000-0002-4694-4299}},
	Pages = {{2378-2381}},
	Researcherid-Numbers = {{Engelbrekt, Christian/A-8281-2012 Jensen, Knud/D-1145-2016 Thulstrup, Peter/C-5598-2013 zhao, jianming/L-2598-2016 Christensen, Niels Johan/J-3820-2014 }},
	Title = {{Construction of Insulin 18-mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites}},
	Unique-Id = {{ISI:000369970500011}},
	Volume = {{55}},
	Year = {{2016}},
	Bdsk-Url-1 = {http://dx.doi.org/10.1002/anie.201509088%7D}}
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