Structural investigation of the interactions of biotinylruthenocene with avidin.
Chem Biol Interact
; 204(1): 6-12, 2013 Jun 25.
Article
en En
| MEDLINE
| ID: mdl-23603015
The crystal structure of avidin, a protein from hen egg white, was determined in the form of a complex with biotinylruthenocene. This biotin-derived organometallic ligand is a potential anticancer agent for targeted therapy based upon avidin-biotin technology. Isothermal titration calorimetry experiments, involving avidin complexes with biotin (vitamin H or B7) derivatives, show differences in their affinity to the protein in comparison to its avidin-biotin complex, the strongest known biochemical interaction in Nature. The crystal structure of the first complex of avidin with biotinylruthenocene, determined at 2.5Å resolution (PDB: 4I60), shows unique interactions of the ruthenocene moiety with avidin. Biotin derivatives exhibit weaker affinity to avidin then biotin, which allows their wider use in biotechnology. The specific properties of biotinylruthenocene and the knowledge of its interactions with avidin may be useful in biochemical, medical, and nanotechnological applications.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Compuestos Organometálicos
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Biotina
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Avidina
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Complejos de Coordinación
Idioma:
En
Revista:
Chem Biol Interact
Año:
2013
Tipo del documento:
Article
País de afiliación:
Polonia
Pais de publicación:
Irlanda