In:
Angewandte Chemie, Wiley, Vol. 128, No. 7 ( 2016-02-12), p. 2424-2427
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.
Type of Medium:
Online Resource
ISSN:
0044-8249
,
1521-3757
DOI:
10.1002/ange.201509088
Language:
English
Publisher:
Wiley
Publication Date:
2016
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