Controlled self-assembly of re-engineered insulin by Fe(II).
Chemistry
; 17(26): 7198-204, 2011 Jun 20.
Article
en En
| MEDLINE
| ID: mdl-21626587
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
2,2'-Dipiridil
/
Compuestos Ferrosos
/
Insulina
Idioma:
En
Revista:
Chemistry
Asunto de la revista:
QUIMICA
Año:
2011
Tipo del documento:
Article
País de afiliación:
Dinamarca
Pais de publicación:
Alemania