title: Coupling biomolecules to fullerenes through a molecular adapter.
abstract: 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.
authors.affiliation: Department of Chemistry and Advanced Carbon Materials Center, University of Kentucky, Lexington, Kentucky 40506-0055, USA.
authors.forename: Marcello
authors.initials: M
authors.lastname: Capaccio
authors.forename: Vasilis G
authors.initials: VG
authors.lastname: Gavalas
authors.forename: Mark S
authors.initials: MS
authors.lastname: Meier
authors.forename: John E
authors.initials: JE
authors.lastname: Anthony
authors.forename: Leonidas G
authors.initials: LG
authors.lastname: Bachas
mesh_terms: 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
chemical_list: D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized; D037741:Fullerenes; D011506:Proteins; D019809:Streptavidin; D000469:Alkaline Phosphatase