Coupling biomolecules to fullerenes through a molecular adapter.
A novel biotinylated fullerene has been synthesized to facilitate the attachment of biotin-conjugated proteins to C(60) through the use of streptavidin as a molecular adapter. The strong biotin-streptavidin interaction enables the attachment of fullerenes to streptavidin and, because of the availability of four biotin-binding sites on streptavidin, to biotinylated biomolecules. The feasibility of this approach is demonstrated by using biotinylated alkaline phosphatase. Due to the insolubility of fullerenes in aqueous media, the immobilized enzyme can be eventually recovered by simple centrifugation with no significant loss in activity.
Capaccio
Marcello
M
Department of Chemistry and Advanced Carbon Materials Center, University of Kentucky, Lexington, Kentucky 40506-0055, USA.
Gavalas
Vasilis G
VG
Meier
Mark S
MS
Anthony
John E
JE
Bachas
Leonidas G
LG
D000469:Alkaline Phosphatase; D019921:Biotinylation; D003432:Cross-Linking Reagents / Q000737:chemistry; D004800:Enzymes, Immobilized / Q000737:chemistry; D037741:Fullerenes / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D019809:Streptavidin / Q000737:chemistry
D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized; D037741:Fullerenes; D011506:Proteins; D019809:Streptavidin; D000469:Alkaline Phosphatase