Controlled Self-Assembly of Re-engineered Insulin by FeII

被引：22

作者：

Munch, Henrik K. ^{[1
]}

Heide, Soren Thiis ^{[1
]}

Christensen, Niels Johan ^{[1
]}

Hoeg-Jensen, Thomas ^{[2
]}

Thulstrup, Peter W. ^{[1
]}

Jensen, Knud J. ^{[1
]}

机构：

[1] Univ Copenhagen, IGM, Fac Life Sci, DK-1871 Frederiksberg, Denmark

[2] Novo Nordisk AS, DK-2760 Malov, Denmark

来源：

CHEMISTRY-A EUROPEAN JOURNAL | 2011年 / 17卷 / 26期

关键词：

bipyridine; insulin; iron; protein-protein interactions; self-assembly; COILED-COIL; PROTEIN; PEPTIDE; LIGAND; METALLOPROTEINS; RUTHENIUM(II); DIMERIZATION; COMPLEXES; FRAMEWORK; ANALOGS;

D O I：

10.1002/chem.201100495

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：7198 / 7204

页数：7

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