Controlled self-assembly of re-engineered insulin by Fe(II) |
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Authors: | Munch Henrik K Heide Søren Thiis Christensen Niels Johan Hoeg-Jensen Thomas Thulstrup Peter W Jensen Knud J |
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Institution: | IGM, Faculty of Life Sciences, University of Copenhagen, Thorvaldsensvej 40, 1871 Frederiksberg, Denmark. |
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Abstract: | Self-assembly of proteins mediated by metal ions is crucial in biological systems and a better understanding and novel strategies for its control are important. An abiotic metal ion ligand in a protein offers the prospect of control of the oligomeric state, if a selectivity over binding to the native side chains can be achieved. Insulin binds Zn(II) to form a hexamer, which is important for its storage in vivo and in drug formulations. We have re-engineered an insulin variant to control its self-assembly by covalent attachment of 2,2'-bipyridine. The use of Fe(II) provided chemoselective binding over the native site, forming a homotrimer in a reversible manner, which was easily followed by the characteristic color of the Fe(II) complex. This provided the first well-defined insulin trimer and the first insulin variant for which self-assembly can be followed visually. |
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Keywords: | bipyridine insulin iron protein–protein interactions self‐assembly |
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