Albumin-binding surfaces: synthesis and characterization.
J Biomater Sci Polym Ed
; 9(11): 1207-25, 1998.
Article
en En
| MEDLINE
| ID: mdl-9860181
The nature of the proteinaceous film deposited on a biomaterial surface following implantation is a key determinant of the subsequent biological response. To achieve selectivity in the formation of this film, monoclonal antibodies have been coupled to a range of solid substrates using avidin-biotin technology. Antibody clones varied in their antigen-binding activity following insertion of biotin groups into lysine residues. Biotinylated antibodies coupled to solid substrates via an immobilized avidin bridge retained their biological activity. During immobilization of avidin a significant proportion of the protein molecules were passively adsorbed rather than covalently attached to the surface. This loosely bound material could be removed by stringent elution procedures which resulted in a surface density of 5.4 pmol avidin cm(-2). Although these conditions would be harsh enough to denature monoclonal antibodies, they did not destroy the biotin-binding activity of the residual surface-coupled avidin, enabling the subsequent immobilization of biotinylated antibodies. The two-step immobilization technique allowed the use of gentle protein modification procedures, reduced the risk of surface-induced denaturation and removed loosely bound material from the surface. The versatility of the technique encourages its application to a wide range of immobilization systems where retention of biological activity is a key requirement.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Albúmina Sérica
/
Materiales Biocompatibles Revestidos
/
Anticuerpos Monoclonales
Límite:
Animals
/
Female
/
Humans
Idioma:
En
Revista:
J Biomater Sci Polym Ed
Asunto de la revista:
ENGENHARIA BIOMEDICA
Año:
1998
Tipo del documento:
Article
País de afiliación:
Australia
Pais de publicación:
Reino Unido