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Construction of Insulin 18‐mer Nanoassemblies Driven by Coordination to Iron(II) and Zinc(II) Ions at Distinct Sites
Author(s) -
Munch Henrik K.,
Nygaard Jesper,
Christensen Niels Johan,
Engelbrekt Christian,
Østergaard Mads,
Porsgaard Trine,
HoegJensen Thomas,
Zhang Jingdong,
Arleth Lise,
Thulstrup Peter W.,
Jensen Knud J.
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201509088
Subject(s) - chemistry , random hexamer , metal ions in aqueous solution , crystallography , ligand (biochemistry) , metal , zinc , ion , organic chemistry , receptor , biochemistry
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.