Molecular recognition of avidin on biotin-functionalized gold surfaces detected by FT-IRRAS and use of metal carbonyl probes.
J Colloid Interface Sci
; 245(1): 204-7, 2002 Jan 01.
Article
en En
| MEDLINE
| ID: mdl-16290351
Fourier transform infrared reflection-absorption spectroscopy (FT-IRRAS) was successively used to monitor the covalent immobilization of biotin molecules onto a planar gold substrate covered with a self-assembled monolayer of cystamine and to transduce the molecular recognition of avidin and biotin. This detection was greatly facilitated and made selective by the labeling of avidin and of biotin with various transition metal carbonyl probes. The binding of avidin to the surface was optimized by blocking the nonspecific binding sites by adsorption of an unrelated protein, bovine serum albumin. This work exemplifies the feasibility of detecting biomolecular associations involving molecules of any size at a liquid/solid interface by using a simple and accessible surface analysis technique.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Compuestos Organometálicos
/
Biotina
/
Avidina
/
Oro
Tipo de estudio:
Diagnostic_studies
Idioma:
En
Revista:
J Colloid Interface Sci
Año:
2002
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos